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Human serum albumin
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human serum albumin
PDB rendering based on 1e7h.
Identifiers
Symbol
ALB
Entrez
213
HUGO
399
OMIM
103600
PDB
1E7H
RefSeq
NM_000477
UniProt
P02768
Other data
Locus
Chr. 4 q13.3
Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma; it constitutes about half of serum protein. It is produced in the liver. It is soluble and monomeric.
Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains oncotic pressure, among other functions.
Albumin is synthesized in the liver as preproalbumin, which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.
The reference range for albumin concentrations in serum is approximately 35 - 50 g/L (3.5 - 5.0 g/dL).[1] It has a serum half-life of approximately 20 days. It has a molecular mass of 66.5 kDa.
The gene for albumin is located on chromosome 4 and mutations in this gene can result in anomalous proteins. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly(A) addition site. It is split into 15 exons that are symmetrically placed within the 3 domains thought to have arisen by triplication of a single primordial domain.
Contents
[hide]
1 Function
2 Measurement
3 Reference ranges
4 Pathology
4.1 Hypoalbuminemia
4.2 Hyperalbuminemia
4.3 Therapeutic uses
5 Glycation
6 Oxidation
7 Loss via kidneys
8 Amino acid sequence
9 Interactions
10 See also
11 References
12 Further reading
13 External links
Function[edit]
Maintains oncotic pressure
Transports thyroid hormones
Transports other hormones, in particular, ones that are fat-soluble
Transports fatty acids ("free" fatty acids) to the liver and to myocytes for utilization of energy
Transports unconjugated bilirubin
Transports many drugs; serum albumin levels can affect the half-life of drugs
Competitively binds calcium ions (Ca2+)
Serum albumin, as a negative acute-phase protein, is down-regulated in inflammatory states. As such, it is not a valid marker of nutritional status; rather, it is a marker of an inflammatory state
Prevents photodegradation of folic acid
Measurement[edit]
Serum albumin is commonly measured by recording the change in absorbance upon binding to a dye such as bromocresol green or bromocresol purple.[2]
Reference ranges[edit]
Serum albumin concentration is typically 35 - 50 g/L (3.5 - 5.0 g/dL)[1]
Pathology[edit]
Hypoalbuminemia[edit]
Hypoalbuminemia is a low blood albumin levels.[3] This can be caused by:
Liver disease; cirrhosis of the liver is most common
Excess excretion by the kidneys (as in nephrotic syndrome)
Excess loss in bowel (protein-losing enteropathy, e.g., Ménétrier's disease)
Burns (plasma loss in the absence of skin barrier)
Redistribution (hemodilution [as in pregnancy], increased vascular permeability or decreased lymphatic clearance)
Acute disease states (referred to as a negative acute-phase protein)
Malnutrition and wasting[4]
Mutation causing analbuminemia (very rare)
Hyperalbuminemia[edit]
Hyperalbuminemia is an increased concentration of albumin in the blood.[5] Typically, this condition is due to abrupt dehydration.[5]
Chronic dehydration needs to be treated with zinc as well as with water[citation needed]. Zinc reduces cell swelling caused by decreased intake of water (hypotonicity) and also increases retention of salt. In the dehydrated state, the body has too high an osmolarity and, it appears, discards zinc to prevent this. Zinc also regulates transport of the cellular osmolyte taurine, and albumin is known to increase cellular taurine absorption. Zinc has been shown to increase retinol (vitamin A) production from beta-carotene, and in lab experiments retinol reduced human albumin production.[6] It is possible that a retinol (vitamin A) deficiency alone could cause albumin levels to become raised. Patients recovering from chronic dehydration may develop dry eyes as the body uses up its vitamin A store. Retinol causes cells to swell with water (this is most likely one reason that too much vitamin A is toxic).[7] Hyperalbuminemia is also associated with high protein diets.[8]
Therapeutic uses[edit]
Human albumin solution or HSA is available for medical use, usually at concentrations of 5-25%.
Human albumin is often used to replace lost fluid and help restore blood volume in trauma, burns and surgery patients. A Cochrane systematic review[9] of 37 trials found no evidence that albumin, compared with cheaper alternatives such as saline, reduces the risk of dying.
Human serum albumin has been used as a component of a frailty index.[4]
It has not been shown to give better results than other fluids when used simply to replace volume, but is frequently used in conditions where loss of albumin is a major problem, such as liver disease with ascites.
Glycation[edit]
It has been known for a long time that human blood proteins like hemoglobin[10] and serum albumin[11][12] may undergo a slow non-enzymatic glycation, mainly by formation of a Schiff base between ε-amino groups of lysine (and sometimes arginine) residues and glucose molecules in blood (Maillard reaction). This reaction can be inhibited in the presence of antioxidant agents.[13] Although this reaction may happen normally,[11] elevated glycoalbumin is observed in diabetes mellitus.[12]
Glycation has the potential to alter the biological structure and function of the serum albumin protein.[14][15][16][17]
Moreover, the glycation can result in the formation of Advanced Glycation End-Products (AGE), which result in abnormal biological effects. Accumulation of AGEs leads to tissue damage via alteration of the structures and functions of tissue proteins, stimulation of cellular responses, through receptors specific for AGE-proteins, and generation of reactive oxygen intermediates. AGEs also react with DNA, thus causing mutations and DNA transposition. Thermal processing of proteins and carbohydrates brings major changes in allergenicity. AGEs are antigenic and represent many of the important neoantigens found in cooked or stored foods.[18] They also interfere with the normal product of nitric oxide in cells.[19]
Although there are several lysine and arginine residues in the serum albumin structure, very few of them can take part in the glycation reaction.[12][20] It is not clear exactly why only these residues are glycated in serum albumin, but it is suggested that non-covalent binding of glucose to serum albumin prior to the covalent bond formation might be the reason.[21]
Oxidation[edit]
The albumin is the predominant protein in most body fluids, its Cys34 represents the largest fraction of free thiols within body. The albumin Cys34 thiol exists in both reduced and oxidized forms.[22] In plasma of healthy young adults, 70%-80% of total HSA contains the free sulfhydryl group of Cys34 in a reduced form or mercaptoalbumin (HSA-SH).[23] However, in pathological states characterized by oxidative stress and during the aging process, the oxidized form, or non-mercaptoalbumin (HNA), could predominate [24] . The albumin thiol reacts with radical hydroxyl (.OH), hydrogen peroxide (H2O2) and the reactive nitrogen species as peroxynitrite (ONOO.), and have been shown to oxidize Cys34 to sulfenic acid derivate (HSA-SOH), it can be recycled to mercapto-albumin; however at high concentrations of reactive species leads to the irreversible oxidation to sulfinic (HSA-SO2H) or sulfonic acid (HSA-S3OH) affecting its structure.[25] Presence of reactive oxygen species (ROS), can induce irreversible structural damage and alter protein activities.
Loss via kidneys[edit]
In the healthy kidney, albumin's size and negative electric charge exclude it from excretion in the glomerulus. This is not always the case, as in some diseases including diabetic nephropathy, which can sometimes be a complication of uncontrolled or of longer term diabetes in which proteins can cross the glomerulus. The lost albumin can be detected by a simple urine test.[26] Depending on the amount of albumin lost, a patient may have normal renal function, microalbuminuria, or albuminuria.
Amino acid sequence[edit]
The approximate sequence of human serum albumin is:[27]
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV AASQAALGL
Of the 609 amino acids in this sequence, encoded by the ALB gene and translated to form the precursor protein, only 585 amino acids are observed in the final product present in the blood; the first 24 amino acids (here italicized), including the signal peptide (1–18) and propeptide (19–22, or 19–24[citation needed]) portions, are cleaved after translation.
Interactions[edit]
Human serum albumin has been shown to interact with FCGRT.[28]
See also[edit]
Bovine serum albumin
Serum albumin
References[edit]
^ Jump up to: a b "Harmonisation of Reference Intervals" (PDF). pathologyharmony.co.uk. Pathology Harmony. Retrieved 23 June 2013.
Jump up ^ "Albumin: analyte monograph" (PDF). Association for Clinical Biochemistry and Laboratory Medicine. Archived from the original (PDF) on 13 November 2012. Retrieved 23 June 2013.
Jump up ^ Anderson, Douglas M. (2000). Dorland's illustrated medical dictionary (29. ed.). Philadelphia [u.a.]: Saunders. p. 860. ISBN 0721682618.
^ Jump up to: a b Green P, Woglom AE, Genereux P, Daneault B, Paradis JM, Schnell S, Hawkey M, Maurer MS, Kirtane AJ, Kodali S, Moses JW, Leon MB, Smith CR, Williams M (2012). "The impact of frailty status on survival after transcatheter aortic valve replacement in older adults with severe aortic stenosis: a single-center experience". JACC Cardiovascular Interventions. 5 (9): 974–981. PMC 3717525  . PMID 22995885. doi:10.1016/j.jcin.2012.06.011.
^ Jump up to: a b Walker, edited by H. Kenneth; Hall, W. Dallas; Schlossberg, J. Willis Hurst ; illustrations by Leon; Boyter, Charles H. (1990). Clinical methods : the history, physical, and laboratory examinations (3rd ed.). Boston: Butterworths. p. Chapter 101. ISBN 040990077X. CS1 maint: Extra text: authors list (link)
Jump up ^ Masaki T, Matsuura T, Ohkawa K, Miyamura T, Okazaki I, Watanabe T, Suzuki T (July 2006). "All-trans retinoic acid down-regulates human albumin gene expression through the induction of C/EBPβ-LIP". Biochem. J. 397 (2): 345–53. PMC 1513275  . PMID 16608438. doi:10.1042/BJ20051863.
Jump up ^ Pasantes-Morales H, Wright CE, Gaull GE (December 1984). "Protective effect of taurine, zinc and tocopherol on retinol-induced damage in human lymphoblastoid cells". J. Nutr. 114 (12): 2256–61. PMID 6502269.
Jump up ^ Mutlu EA, Keshavarzian A, Mutlu GM (June 2006). "Hyperalbuminemia and elevated transaminases associated with high-protein diet". Scand. J. Gastroenterol. 41 (6): 759–60. PMID 16716979. doi:10.1080/00365520500442625.
Jump up ^ The Albumin Reviewers (Alderson P, Bunn F, Li Wan Po A, Li L, Pearson M, Roberts I, Schierhout G). Human albumin solution for resuscitation and volume expansion in critically ill patients" Cochrane Database of Systematic Reviews 2004, Issue 4. Art. No.: CD001208. doi:10.1002/14651858.CD001208.pub2.
Jump up ^ Rahbar S (October 1968). "An abnormal hemoglobin in red cells of diabetics". Clin. Chim. Acta. 22 (2): 296–8. PMID 5687098. doi:10.1016/0009-8981(68)90372-0.
^ Jump up to: a b Day JF, Thorpe SR, Baynes JW (February 1979). "Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum". J. Biol. Chem. 254 (3): 595–7. PMID 762083.
^ Jump up to: a b c Iberg N, Flückiger R (October 1986). "Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites". J. Biol. Chem. 261 (29): 13542–5. PMID 3759977.
Jump up ^ Jakus V, Hrnciarová M, Cársky J, Krahulec B, Rietbrock N (1999). "Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidant activity". Life Sci. 65 (18–19): 1991–3. PMID 10576452. doi:10.1016/S0024-3205(99)00462-2.
Jump up ^ Mohamadi-Nejad A, Moosavi-Movahedi AA, Hakimelahi GH, Sheibani N (September 2002). "Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration". Int. J. Biochem. Cell Biol. 34 (9): 1115–24. PMID 12009306. doi:10.1016/S1357-2725(02)00031-6.
Jump up ^ Shaklai N, Garlick RL, Bunn HF (March 1984). "Nonenzymatic glycosylation of human serum albumin alters its conformation and function". J. Biol. Chem. 259 (6): 3812–7. PMID 6706980.
Jump up ^ Mendez DL, Jensen RA, McElroy LA, Pena JM, Esquerra RM (December 2005). "The effect of non-enzymatic glycation on the unfolding of human serum albumin". Arch. Biochem. Biophys. 444 (2): 92–9. PMID 16309624. doi:10.1016/j.abb.2005.10.019.
Jump up ^ Mohamadi-Nejada A, Moosavi-Movahedi AA, Safariana S, Naderi-Maneshc MH, Ranjbarc B, Farzamid B, Mostafavie H, Larijanif MB, Hakimelahi GH, A (July 2002). "The thermal analysis of nonezymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies". Thermochimica Acta. 389 (1–2): 141–151. doi:10.1016/S0040-6031(02)00006-0. CS1 maint: Multiple names: authors list (link)
Jump up ^ Kańska U, Boratyński J (2002). "Thermal glycation of proteins by D-glucose and D-fructose". Arch. Immunol. Ther. Exp. (Warsz.). 50 (1): 61–6. PMID 11916310.
Jump up ^ Rojas A, Romay S, González D, Herrera B, Delgado R, Otero K (February 2000). "Regulation of endothelial nitric oxide synthase expression by albumin-derived advanced glycosylation end products". Circ. Res. 86 (3): E50–4. PMID 10679490. doi:10.1161/01.RES.86.3.e50.
Jump up ^ Garlick RL, Mazer JS (May 1983). "The principal site of nonenzymatic glycosylation of human serum albumin in vivo". J. Biol. Chem. 258 (10): 6142–6. PMID 6853480.
Jump up ^ Marashi SA, Safarian S, Moosavi-Movahedi AA (2005). "Why major nonenzymatic glycation sites of human serum albumin are preferred to other residues?". Med. Hypotheses. 64 (4): 881. PMID 15694713. doi:10.1016/j.mehy.2004.11.007.
Jump up ^ Kawakami A, Kubota K, Yamada N, Tagami U, Takehana T, Sonaka I, Suzuki I, Hirayama K (2006). Identification and characterization of oxidized human serum albumin. FEBS J, 273:3346–3357. Doi: 10.1111/j.1742-4658.2006.05341.x
Jump up ^ Turell L, Carballal L, Botti H, Radi R, Alvarez B. (2009). Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment. Braz J Med Biol Res 42:305-311.
Jump up ^ Rosas-Díaz M, Camarillo-Cadena M, Hernández-Arana A, Ramón-Gallegos E, Medina-Navarro R. (2015). Antioxidant capacity and structural changes of human serum albumin from patients in advanced stages of diabetic nephropathy and the effect of the dialysis. Molecular and Cellular Biochemistry, 404:193-201.
Jump up ^ Matsuyama Y, Terawaki H, Terada T, Era S. (2011). Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease. Clin Exp Nephrol, 13(4):308-315.
Jump up ^ Microalbumin Urine Test
Jump up ^ Universal protein resource accession number P02768 for "Serum albumin" at UniProt.
Jump up ^ Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, Anderson CL (February 2003). "The Major Histocompatibility Complex–related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan". J. Exp. Med. 197 (3): 315–22. PMC 2193842  . PMID 12566415. doi:10.1084/jem.20021829.
Further reading[edit]
Komatsu T, Nakagawa A, Curry S, Tsuchida E, Murata K, Nakamura N, Ohno H (2009). "The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O(2) and CO binding to iron protoporphyrin IX". Org. Biomol. Chem. 7 (18): 3836–41. PMID 19707690. doi:10.1039/b909794e.
Milojevic J, Raditsis A, Melacini G (2009). "Human Serum Albumin Inhibits Aβ Fibrillization through a "Monomer-Competitor" Mechanism". Biophys. J. 97 (9): 2585–94. PMC 2770600  . PMID 19883602. doi:10.1016/j.bpj.2009.08.028.
Silva AM, Hider RC (2009). "Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation". Biochim. Biophys. Acta. 1794 (10): 1449–58. PMID 19505594. doi:10.1016/j.bbapap.2009.06.003.
Otosu T, Nishimoto E, Yamashita S (2010). "Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy". J. Biochem. 147 (2): 191–200. PMID 19884191. doi:10.1093/jb/mvp175.
Blindauer CA, Harvey I, Bunyan KE, Stewart AJ, Sleep D, Harrison DJ, Berezenko S, Sadler PJ (2009). "Structure, Properties, and Engineering of the Major Zinc Binding Site on Human Albumin". J. Biol. Chem. 284 (34): 23116–24. PMC 2755717  . PMID 19520864. doi:10.1074/jbc.M109.003459.
Juárez J, López SG, Cambón A, Taboada P, Mosquera V (2009). "Influence of electrostatic interactions on the fibrillation process of human serum albumin". J Phys Chem B. 113 (30): 10521–9. PMID 19572666. doi:10.1021/jp902224d.
Fu BL, Guo ZJ, Tian JW, Liu ZQ, Cao W (2009). "[Advanced glycation end products induce expression of PAI-1 in cultured human proximal tubular epithelial cells through NADPH oxidase dependent pathway]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 25 (8): 674–7. PMID 19664386.
Ascenzi P, di Masi A, Coletta M, Ciaccio C, Fanali G, Nicoletti FP, Smulevich G, Fasano M (2009). "Ibuprofen Impairs Allosterically Peroxynitrite Isomerization by Ferric Human Serum Heme-Albumin". J. Biol. Chem. 284 (45): 31006–17. PMC 2781501  . PMID 19734142. doi:10.1074/jbc.M109.010736.
Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009). "Defining the Human Deubiquitinating Enzyme Interaction Landscape". Cell. 138 (2): 389–403. PMC 2716422  . PMID 19615732. doi:10.1016/j.cell.2009.04.042.
Curry S (2002). "Beyond expansion: structural studies on the transport roles of human serum albumin". Vox Sang. 83 Suppl 1: 315–9. PMID 12617161. doi:10.1111/j.1423-0410.2002.tb05326.x.
Guo S, Shi X, Yang F, Chen L, Meehan EJ, Bian C, Huang M (2009). "Structural basis of transport of lysophospholipids by human serum albumin". Biochem. J. 423 (1): 23–30. PMID 19601929. doi:10.1042/BJ20090913.
de Jong PE, Gansevoort RT (2009). "Focus on microalbuminuria to improve cardiac and renal protection". Nephron Clin Pract. 111 (3): c204–10; discussion c211. PMID 19212124. doi:10.1159/000201568.
Page TA, Kraut ND, Page PM, Baker GA, Bright FV (2009). "Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids". J Phys Chem B. 113 (38): 12825–30. PMID 19711930. doi:10.1021/jp904475v.
Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E (2008). "The antioxidant properties of serum albumin". FEBS Lett. 582 (13): 1783–7. PMID 18474236. doi:10.1016/j.febslet.2008.04.057.
Wyatt AR, Wilson MR (2010). "Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin". J. Biol. Chem. 285 (6): 3532–9. PMC 2823492  . PMID 19996109. doi:10.1074/jbc.M109.079566.
Cui FL, Yan YH, Zhang QZ, Qu GR, Du J, Yao XJ (2010). "A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling". J Mol Model. 16 (2): 255–62. PMID 19588173. doi:10.1007/s00894-009-0548-4.
Caridi G, Dagnino M, Simundic AM, Miler M, Stancic V, Campagnoli M, Galliano M, Minchiotti L (2010). "Albumin Benkovac (c.1175 A > G; p.Glu392Gly): a novel genetic variant of human serum albumin". Translational Research. 155 (3): 118–9. PMID 20171595. doi:10.1016/j.trsl.2009.10.001.
Deeb O, Rosales-Hernández MC, Gómez-Castro C, Garduño-Juárez R, Correa-Basurto J (2010). "Exploration of human serum albumin binding sites by docking and molecular dynamics flexible ligand-protein interactions". Biopolymers. 93 (2): 161–70. PMID 19785033. doi:10.1002/bip.21314.
Karahan SC, Koramaz I, Altun G, Uçar U, Topbaş M, Menteşe A, Kopuz M (2010). "Ischemia-modified albumin reduction after coronary bypass surgery is associated with the cardioprotective efficacy of cold-blood cardioplegia enriched with N-acetylcysteine: a preliminary study". Eur Surg Res. 44 (1): 30–6. PMID 19955769. doi:10.1159/000262324.
Jin C, Lu L, Zhang RY, Zhang Q, Ding FH, Chen QJ, Shen WF (2009). "Association of serum glycated albumin, C-reactive protein and ICAM-1 levels with diffuse coronary artery disease in patients with type 2 diabetes mellitus". Clin. Chim. Acta. 408 (1–2): 45–9. PMID 19615354. doi:10.1016/j.cca.2009.07.003.
External links[edit]
Human Albumin structure in the Protein data bank
Human Albumin information in the Swis-Prot/TrEMBL database
Human Serum Albumin on the Human Protein Reference Database
Albumin binding prediction
Albumin at Lab Tests Online
Albumin: analyte monograph from the Association for Clinical Biochemistry and Laboratory Medicine
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PDB gallery
1ao6: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
1bj5: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID
1bke: HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-IODOBENZOIC ACID
1bm0: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
1e78: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
1e7a: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL ANESTHETIC PROPOFOL
1e7b: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL ANESTHETIC HALOTHANE
1e7c: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE GENERAL ANESTHETIC HALOTHANE
1e7e: HUMAN SERUM ALBUMIN COMPLEXED WITH DECANOIC ACID (CAPRIC ACID)
1e7f: HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID (LAURIC ACID)
1e7g: HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID
1e7h: HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID (PALMITIC ACID)
1e7i: HUMAN SERUM ALBUMIN COMPLEXED WITH OCTADECANOIC ACID (STEARIC ACID)
1gni: HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-9-OCTADECENOIC ACID (OLEIC ACID)
1gnj: HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)
1h9z: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE R-(+) ENANTIOMER OF WARFARIN
1ha2: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE S-(-) ENANTIOMER OF WARFARIN
1hk1: HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)
1hk2: HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)
1hk3: HUMAN SERUM ALBUMIN MUTANT R218P COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE)
1hk4: HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)
1hk5: HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)
1n5u: X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME
1o9x: HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC ACID) AND HEMIN
1tf0: Crystal structure of the GA module complexed with human serum albumin
1uor: X-RAY STUDY OF RECOMBINANT HUMAN SERUM ALBUMIN. PHASES DETERMINED BY MOLECULAR REPLACEMENT METHOD, USING LOW RESOLUTION STRUCTURE MODEL OF TETRAGONAL FORM OF HUMAN SERUM ALBUMIN
1ysx: Solution structure of domain 3 from human serum albumin complexed to an anti-apoptotic ligand directed against Bcl-xL and Bcl-2
2bx8: HUMAN SERUM ALBUMIN COMPLEXED WITH AZAPROPAZONE
2bxa: HUMAN SERUM ALBUMIN COMPLEXED WITH 3-CARBOXY-4-METHYL-5-PROPYL-2-FURANPROPANOIC ACID (CMPF)
2bxb: HUMAN SERUM ALBUMIN COMPLEXED WITH OXYPHENBUTAZONE
2bxc: HUMAN SERUM ALBUMIN COMPLEXED WITH PHENYLBUTAZONE
2bxd: HUMAN SERUM ALBUMIN COMPLEXED WITH WARFARIN
2bxe: HUMAN SERUM ALBUMIN COMPLEXED WITH DIFLUNISAL
2bxf: HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM
2bxg: HUMAN SERUM ALBUMIN COMPLEXED WITH IBUPROFEN
2bxh: HUMAN SERUM ALBUMIN COMPLEXED WITH INDOXYL SULFATE
2bxi: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND AZAPROPAZONE
2bxk: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND INDOMETHACIN
2bxl: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND 3,5-DIIODOSALICYLIC ACID
2bxm: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND INDOMETHACIN
2bxn: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND IODIPAMIDE
2bxo: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND OXYPHENBUTAZONE
2bxp: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE
2bxq: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, PHENYLBUTAZONE AND INDOMETHACIN
2i2z: Human serum albumin complexed with myristate and aspirin
2i30: Human serum albumin complexed with myristate and salicylic acid
[show]
v
t
e
Proteins: Globular proteins
Serum globulins
Alpha globulins
serpins:
alpha-1 (Alpha 1-antichymotrypsin, Alpha 1-antitrypsin)
alpha-2 (Alpha 2-antiplasmin)
Antithrombin (Heparin cofactor II)
carrier proteins:
alpha-1 (Transcortin)
alpha-2 (Ceruloplasmin)
Retinol binding protein
other:
alpha-1 (Orosomucoid)
alpha-2 (alpha-2-Macroglobulin, Haptoglobin)
Beta globulins
carrier proteins:
Sex hormone-binding globulin
Transferrin
other:
Angiostatin
Hemopexin
Beta-2 microglobulin
Factor H
Plasminogen
Properdin
Gamma globulin
Immunoglobulins
Other
Fibronectin (fFN: Fetal fibronectin)
Macroglobulin/Microglobulin
Transcobalamin
Other globulins
Beta-lactoglobulin
Lactoferrin
Thyroglobulin
Alpha-lactalbumin
11S globulin family (seeds)
7S globulin family (seeds)
Albumins
Egg white
Conalbumin
Ovalbumin
Avidin
Serum albumin
Human serum albumin
Bovine serum albumin
Prealbumin
Other
C-reactive protein
Lactalbumin (Alpha-lactalbumin)
Parvalbumin
Ricin
Edestin
see also disorders of globin and globulin proteins
[show]
v
t
e
Acute-phase proteins
Amyloid
SAP
SAA
Other positive
Alpha 1-antichymotrypsin
Alpha 1-antitrypsin
Alpha 2-macroglobulin
C-reactive protein
Ceruloplasmin
C3
Ferritin
Fibrin
Haptoglobin
Hemopexin
Orosomucoid
Negative
Serum albumin
Transferrin
[show]
v
t
e
Nuclear receptor modulators
AhR
Agonists: Arachidonic acid metabolites (e.g., lipoxin A4, prostaglandin G2)
Dietary carotenoids
Flutamide
Halogenated aromatic hydrocarbons (e.g., polychlorinated dibenzodioxins (e.g., TCDD), dibenzofurans, biphenyls)
Modified low-density lipoproteins
Polycyclic aromatic hydrocarbons (e.g., 3-methylcholanthrene, benzo[a]pyrene, benzanthracenes, benzoflavones (e.g., beta-naphthoflavone))
Tapinarof
Tetrapyroles (e.g., bilirubin)
Tryptophan derivatives (e.g., indigo dye, indirubin)
Antagonists: 7-Ketocholesterol
CAR
See here instead.
ERR
ERRα
Agonists: 6,3′,4′-Trihydroxyflavone
Biochanin A
Cholesterol
Daidzein
Genistein
Antagonists: Diethylstilbestrol
XCT-790
ERRβ
Agonists: DY-131 (GSK-9089)
GSK-4716 (GW-4716)
Antagonists: 4-Hydroxytamoxifen (afimoxifene)
Diethylstilbestrol
ERRγ
Agonists: Bisphenol A
DY-131 (GSK-9089)
GSK-4716 (GW-4716)
Antagonists: 4-Hydroxytamoxifen (afimoxifene)
Diethylstilbestrol
FXR
Agonists: Bile acids
Cafestol
Chenodeoxycholic acid
Fexaramine
GW-4064
Obeticholic acid
Antagonists: Guggulsterone
LXR
Agonists: 22R-Hydroxycholesterol
24S-Hydroxycholesterol
27-Hydroxycholesterol
Cholestenoic acid
DMHCA
GW-3965
Hypocholamide
T-0901317
Antagonists: Efavirenz
PPAR
See here instead.
PXR
See here instead.
Retinoid
See here instead.
SHR
AR
See here instead.
ER
See here instead.
PR
See here instead.
GR
See here instead.
MR
See here instead.
THR
See here instead.
VDR
See here instead.
See also
Receptor/signaling modulators
Leukotriene signaling modulators
Prostanoid signaling modulators
Retrieved from "https://en.wikipedia.org/w/index.php?title=Human_serum_albumin&oldid=798255499"
Categories:
Genes on human chromosome 4
Blood proteins
Liver function tests
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values: 1ao6: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

values: min-height:6.1em;width:187px;line-height:1.3em;padding:2px 6px 1px 6px;margin:0px;border:none;border-width:0px

values: 1bj5: HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID

values: 1bm0: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

values: 1e78: CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

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values: 2bxc: HUMAN SERUM ALBUMIN COMPLEXED WITH PHENYLBUTAZONE

values: 2bxd: HUMAN SERUM ALBUMIN COMPLEXED WITH WARFARIN

values: 2bxe: HUMAN SERUM ALBUMIN COMPLEXED WITH DIFLUNISAL

values: 2bxf: HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM

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text:
Let 'Em In
From Wikipedia, the free encyclopedia
Jump to: navigation, search
"Let 'Em In"
German sleeve
Single by Wings
from the album Wings at the Speed of Sound
B-side
"Beware My Love"
Released
23 July 1976
Format
7", 12"
Recorded
4 February 1976, Abbey Road Studios, London
Genre
Soft rock
Length
5:10
Label
MPL Communications (UK)
MPL Communications/Capitol (US)
Songwriter(s)
Paul McCartney, Linda McCartney
Producer(s)
Paul McCartney
Wings singles chronology
"Silly Love Songs"
(1976) "Let 'Em In"
(1976) "Maybe I'm Amazed"
(1977)
"Silly Love Songs"
(1976) "Let 'Em In"
(1976) "Maybe I'm Amazed"
(1977)
Audio sample
file
help
Wings at the Speed of Sound track listing
11 tracks [show]
Side one
"Let 'Em In"
"The Note You Never Wrote"
"She's My Baby"
"Beware My Love"
"Wino Junko"
Side two
"Silly Love Songs"
"Cook of the House"
"Time to Hide"
"Must Do Something About It"
"San Ferry Anne"
"Warm and Beautiful"
"Let 'Em In" is a song by Wings from their 1976 album Wings at the Speed of Sound. It was written and sung by Paul McCartney and reached the top 3 in the United Kingdom, the United States and Canada. It was a No. 2 hit in the UK; in the U.S. it was a No. 3 pop hit and No. 1 easy listening hit.[1][2][3] In Canada, the song was No. 3 for three weeks on the pop chart and No. 1 for three weeks on the MOR chart of RPM magazine. The single was certified Gold by the Recording Industry Association of America for sales of over one million copies.[4] It can also be found on McCartney's 1987 compilation album, All the Best! A demo of the song, featuring Denny Laine on lead vocal, was included as a bonus track on the Archive Collection reissue of Wings at the Speed of Sound.
The song starts with the sound of a vibraphone, chiming the first eight notes from the Westminster Quarters, before the rhythm begins. The lyric name-checks several famous people as well as McCartney's paternal aunt Gin and his brother Michael, and Linda McCartney's brother John. Phil and Don Everly (known as the Everly Brothers) are named along with Martin Luther.[5] Uncle Ernie is named; this was the character Ringo Starr sang in the London Symphony Orchestra's recording of the Who's Tommy.[6] "Let 'Em In" is noted for the false fade out, which, however, becomes loud for the last two notes of the song. The song makes use of the piano, drums, brass, including a trombone solo, and wind instruments, featuring flutes, plus backup vocals from Linda and other members of Wings.[7]
Contents
[hide]
1 Release
2 Track listings
3 Chart performance
3.1 Weekly charts
3.2 Year-end charts
4 Cover versions
5 See also
6 References
7 External links
Release[edit]
The song was released worldwide as a 7" single, except in France where it was released as 12" single (the first-ever McCartney 12") with both sides labelled "Special Disco Mix".[8]
It was included on the compilation album Wings Greatest (1978), as well as the Paul McCartney compilation albums All the Best! (1987) and Wingspan: Hits and History (2001).
Track listings[edit]
7" single (R 6015)
"Let 'Em In" – 5:08
"Beware My Love" – 6:05
12" single (2C 052-98.062 y)[A]
"Let 'Em In" (Special Disco Mix) – 5:08
"Beware My Love" (Special Disco Mix) – 6:05
A ^ Released in France only.
Chart performance[edit]
Weekly charts[edit]
Chart (1976)
Peak
position
Australia 65
Canada Top Singles[9] 3
Canada Adult Contemporary 1
Germany 29
Netherlands 25
New Zealand 13
UK 3
US Billboard Hot 100[10] 3
US Billboard Adult Contemporary 1
US Cash Box Top 100[10] 1
Year-end charts[edit]
Chart (1976)
Rank
Australia[11] 188
Canada[12] 46
UK 29
US Billboard Hot 100[13] 66
Cover versions[edit]
The song was covered in 1977 by Billy Paul, substituting a list of notable African-American figures such as Malcolm X and Louis Armstrong in lieu of the people named in the original. This version reached No. 26 on the UK charts.[5]
See also[edit]
List of number-one adult contemporary singles of 1976 (U.S.)
References[edit]
Jump up ^ Whitburn, Joel (2002). Top Adult Contemporary: 1961-2001. Record Research. p. 163.
Jump up ^ "Paul McCartney Charts and Awards". allmusic. Retrieved 13 October 2011.
Jump up ^ "Official Charts: Paul McCartney". The Official UK Charts Company. Retrieved 13 October 2011.
Jump up ^ "riaa.com". riaa.com. Archived from the original on 24 September 2015. Retrieved 2014-02-03.
^ Jump up to: a b Womack, Kenneth (2014). The Beatles Encyclopedia: Everything Fab Four. ABC-CLIO. p. 536. ISBN 9780313391729.
Jump up ^ "1972 All-Star Orchestral Version of The Who's "Tommy" to Be Reissued Next Month". ABC News Radio. 2015-08-11. Retrieved 2016-04-12.
Jump up ^ Benitez, Vince Perez (2010). The Words and Music of Paul McCartney: The Solo Years. ABC-CLIO. pp. 71–2. ISBN 9780313349690.
Jump up ^ "Let 'Em In". JPGR. 2000. Retrieved 25 September 2013.
Jump up ^ http://www.bac-lac.gc.ca/eng/discover/films-videos-sound-recordings/rpm/Pages/image.aspx?Image=nlc008388.4289a&URLjpg=http%3a%2f%2fwww.collectionscanada.gc.ca%2fobj%2f028020%2ff4%2fnlc008388.4289a.gif&Ecopy=nlc008388.4289a
^ Jump up to: a b Whitburn, Joel (2015). The Comparison Book. Menonomee Falls, Wisconsin: Record Research Inc. p. 333. ISBN 978-0-89820-213-7.
Jump up ^ David Kent's "Australian Chart Book 1970-1992" Archived 5 March 2016 at Archive.is
Jump up ^ "Top Singles – Volume 26, No. 14 & 15, January 08 1977". RPM. Library and Archives Canada. Retrieved March 13, 2016.
Jump up ^ "Pop Singles" Billboard December 25, 1976: Talent in Action-6
Preceded by
"You'll Never Find Another Love Like Mine" by Lou Rawls Billboard Adult Contemporary number one single
August 7, 1976 Succeeded by
"If You Know What I Mean" by Neil Diamond
External links[edit]
Lyrics of this song at MetroLyrics
[show]
v
t
e
Wings
Paul McCartney
Linda McCartney
Denny Laine
Denny Seiwell
Henry McCullough
Jimmy McCulloch
Geoff Britton
Joe English
Laurence Juber
Steve Holley
Studio albums
Wild Life (1971)
Red Rose Speedway (1973)
Band on the Run (1973)
Venus and Mars (1975)
Wings at the Speed of Sound (1976)
London Town (1978)
Back to the Egg (1979)
Live albums
Wings over America (1976)
Compilation albums
Wings Greatest (1978)
Cold Cuts (unreleased)
Wingspan: Hits and History (2001)
Singles
1972
"Give Ireland Back to the Irish"
"Mary Had a Little Lamb" / "Little Woman Love"
"Hi, Hi, Hi" / "C Moon"
1973
"My Love" / "The Mess"
"Live and Let Die" / "I Lie Around"
"Helen Wheels" / "Country Dreamer"
"Mrs. Vandebilt" / "Bluebird"
"Jet" / "Mamunia" (early US pressings)
"Jet" / "Let Me Roll It"
1974
"Band on the Run" / "Zoo Gang" (UK)
"Band on the Run" / "Nineteen Hundred and Eighty-Five" (US)
"Walking in the Park with Eloise" / "Bridge Over the River Suite" (as The Country Hams)
"Junior's Farm" / "Sally G"
1975
"Listen to What the Man Said" / "Love in Song"
"Letting Go" / "You Gave Me the Answer"
"Venus and Mars/Rock Show" / "Magneto and Titanium Man"
1976
"Silly Love Songs" / "Cook of the House"
"Let 'Em In" / "Beware My Love"
1977
"Maybe I'm Amazed" (live) / "Soily" (live)
"Seaside Woman" / "B Side to Seaside" (as Suzy and the Red Stripes)
"Mull of Kintyre" / "Girls' School"
1978
"With a Little Luck" / "Backwards Traveller"/"Cuff Link"
"I've Had Enough" / "Deliver Your Children"
"London Town" / "I'm Carrying"
1979
"Goodnight Tonight" / "Daytime Nighttime Suffering"
"Old Siam, Sir" / "Spin It On"
"Getting Closer" / "Spin It On" (US)
"Getting Closer" / "Baby's Request" (UK)
"Arrow Through Me" / "Old Siam, Sir" (US)
"Rockestra Theme" / "Old Siam, Sir" (Europe)
1980
"Coming Up (Live at Glasgow)" / "Lunch Box"/"Odd Sox"
Tours
Wings University Tour (1972)
Wings Over Europe Tour (1972)
Wings 1973 UK Tour (May 1973)
Wings Over the World tour (1975-1976)
Wings UK Tour 1979 (1979)
Concerts for the People of Kampuchea (1979)
Filmography
Wings Over the World (1979)
Concert for Kampuchea (1980)
Rockshow (1980)
Back to the Egg (1981)
Wingspan – An Intimate Portrait (2001)
Related articles
Discography
Songs
The Beatles
Ginger Baker's Air Force
Japanese Tears
The Moody Blues
Standard Time
Suzy and the Red Stripes
Small Faces
The Oriental Nightfish
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Paul McCartney
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Rusty Anderson
Brian Ray
Abe Laboriel, Jr.
Linda McCartney
Hamish Stuart
Robbie McIntosh
Chris Whitten
Blair Cunningham
Studio albums
McCartney
Ram (with Linda McCartney)
McCartney II
Tug of War
Pipes of Peace
Give My Regards to Broad Street
Press to Play
Снова в СССР
Flowers in the Dirt
Off the Ground
Flaming Pie
Run Devil Run
Driving Rain
Chaos and Creation in the Backyard
Memory Almost Full
Kisses on the Bottom
New
with Wings
Wild Life
Red Rose Speedway
Band on the Run
Venus and Mars
Wings at the Speed of Sound
London Town
Back to the Egg
Classical
The Family Way
Thrillington
Paul McCartney's Liverpool Oratorio
Standing Stone
Working Classical
Ecce Cor Meum
Ocean's Kingdom
Electronica
Strawberries Oceans Ships Forest (The Fireman)
Rushes (The Fireman)
Liverpool Sound Collage
Twin Freaks
Electric Arguments (The Fireman)
Live albums
Wings over America
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Unplugged (The Official Bootleg)
Paul Is Live
Back in the U.S.
Back in the World Live
iTunes Festival: London
Amoeba's Secret
Good Evening New York City
Live in Los Angeles
iTunes Live from Capitol Studios
Compilations
Wings Greatest
Cold Cuts (unreleased)
All the Best!
The Paul McCartney Collection
Costello Album (bootleg)
Wingspan: Hits and History
Pure McCartney
Tours
Wings University Tour
Wings Over Europe Tour
Wings 1973 UK Tour
Wings Over the World tour
Wings UK Tour 1979
The Paul McCartney World Tour
The New World Tour
Driving World Tour
Back in the World
2004 Summer Tour
The 'US' Tour
Summer Live '09
Good Evening Europe Tour
Up and Coming Tour
On the Run
Out There
One on One
Filmography
A Hard Day's Night (1964)
Help! (1965)
Magical Mystery Tour (1967)
Yellow Submarine (1968)
Let It Be (1970)
James Paul McCartney (1973)
Wings Over the World (1979)
Rockestra (unreleased) (1979)
Concert for Kampuchea (1980)
Rockshow (1980)
Back to the Egg (1981)
Give My Regards to Broad Street (1984)
Put It There (1990)
Get Back (1991)
Paul Is Live (1993)
In the World Tonight (1997)
Live at the Cavern Club (1999)
Wingspan (2001)
Back in the U.S. (2002)
Paul McCartney in Red Square (2005)
Between Chaos and Creation (2005)
Chaos and Creation at Abbey Road (2005)
The Space Within US (2006)
The McCartney Years (2007)
Good Evening New York City (2009)
The Love We Make (2011)
Related
Articles
Discography
Song list
Awards
Music contributions and appearances
Paul McCartney concerts
Maxi-singles
Paul McCartney: Many Years from Now
MPL Communications
Oobu Joobu
Paul is dead
"Lisa the Vegetarian"
People/Artists
The Quarrymen
The Beatles
Wings
Heather Mills
Personal relationships
Albums
Wide Prairie
A Garland for Linda
Paul McCartney's Glastonbury Groove
Let Us in Americana: The Music of Paul McCartney
A Toot and a Snore in '74
The Art of McCartney
Book
Category
Retrieved from "https://en.wikipedia.org/w/index.php?title=Let_%27Em_In&oldid=806301227"
Categories:
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