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Albumin

January 01, 1970

This article is about the class of proteins. For the substance sometimes called albumen, see egg white. For the specific albumins found in vertebrate bloodstreams, see serum albumin. For other uses, see Albumin (disambiguation).

Albumin is a family of globular proteins, the most common of which are the serum albumins. All of the proteins of the albumin family are water-soluble, moderately soluble in concentrated salt solutions, and experience heat denaturation. Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated. Substances containing albumins are called albuminoids.

Serum albumin family
Structure of serum albumin.[1][2]
Identifiers
SymbolSerum_albumin
PfamPF00273
Pfam clanCL0282
InterProIPR014760
SMARTSM00103
PROSITEPS51438
SCOP21ao6 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1ao6​, 1bj5​, 1bke​, 1bm0​, 1e78​, 1e7a​, 1e7b​, 1e7c​, 1e7e​, 1e7f​, 1e7g​, 1e7h​, 1e7i​, 1gni​, 1gnj​, 1h9z​, 1ha2​, 1hk1​, 1hk2​, 1hk3​, 1hk4​, 1hk5​, 1j78​, 1j7e​, 1kw2​, 1kxp​, 1lot​, 1ma9​, 1n5u​, 1o9x​, 1tf0​, 1uor​, 1ysx​, 2bx8​, 2bxa​, 2bxb​, 2bxc​, 2bxd​, 2bxe​, 2bxf​, 2bxg​, 2bxh​, 2bxi​, 2bxk​, 2bxl​, 2bxm​, 2bxn​, 2bxo​, 2bxp​, 2bxq​, 2i2z​, 2i30​, 2vdb​, 2vue​, 2vuf​, 3b9l​, 3b9m​

A number of blood transport proteins are evolutionarily related in the albumin family, including serum albumin, alpha-fetoprotein, vitamin D-binding protein and afamin.[3][4][5] This family is only found in vertebrates.[6]

Albumins in a less strict sense can mean other proteins that coagulate under certain conditions. See § Other albumin types for lactalbumin, ovalbumin and plant "2S albumin".

Function edit

Albumins in general are transport proteins that bind to various ligands and carry them around.[6] Human types include:

The four canonical human albumins are arranged on chromosome 4 region 4q13.3 in a tandem manner.[10]

Classification edit

Albumins found in animals can be divided into six subfamilies by phylogeny. The Vitamin-D binding proteins occupy families 1–3. The other albumins are mixed among each other in families 4–6. ECM1 is in family 6.[6]

In addition to their medical use, serum albumins are valued in biotechnology. Bovine serum albumin is usually used, although versions from humans and genetically-modified rice are also used to reduce animal cruelty.

Other albumin types edit

A few other proteins are also sometimes called albumins. They are not in the same family as vertebrate albumins:

Structure edit

The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ångströms (250 pm).[1] Albumin is a 65–70 kDa protein.

Albumin comprises three homologous domains that assemble to form a heart-shaped protein.[2] Each domain is a product of two subdomains that possess common structural motifs.[2] The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds.

Forensic uses edit

Worldwide, certain traditional Chinese medicines contain wild bear bile, banned under CITES legislation. Dip sticks, similar to common pregnancy tests, have been developed to detect the presence of bear albumin in traditional medicine products, indicating that bear bile had been used in their creation.[12]

Terminology edit

Albumin is pronounced /ˈælbjʊmɪn/; formed from Latin: albumen[13] "(egg) white; dried egg white".

See also edit

References edit

This article incorporates text from the public domain Pfam and InterPro: IPR014760
  1. ^ a b Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K (June 1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering. 12 (6): 439–46. doi:10.1093/protein/12.6.439. PMID 10388840.
  2. ^ a b c He XM, Carter DC (July 1992). "Atomic structure and chemistry of human serum albumin". Nature. 358 (6383): 209–15. Bibcode:1992Natur.358..209H. doi:10.1038/358209a0. PMID 1630489. S2CID 4353741.
  3. ^ Haefliger DN, Moskaitis JE, Schoenberg DR, Wahli W (October 1989). "Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family". Journal of Molecular Evolution. 29 (4): 344–54. Bibcode:1989JMolE..29..344H. doi:10.1007/BF02103621. PMID 2481749. S2CID 1456034.
  4. ^ Schoentgen F, Metz-Boutigue MH, Jollès J, Constans J, Jollès P (June 1986). "Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 871 (2): 189–98. doi:10.1016/0167-4838(86)90173-1. PMID 2423133.
  5. ^ Lichenstein HS, Lyons DE, Wurfel MM, Johnson DA, McGinley MD, Leidli JC, et al. (July 1994). "Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family". The Journal of Biological Chemistry. 269 (27): 18149–54. doi:10.1016/S0021-9258(17)32429-8. PMID 7517938.
  6. ^ a b c Li S, Cao Y, Geng F (2017). "Genome-Wide Identification and Comparative Analysis of Albumin Family in Vertebrates". Evolutionary Bioinformatics Online. 13: 1176934317716089. doi:10.1177/1176934317716089. PMC 5480655. PMID 28680266.
  7. ^ Farrugia A (January 2010). "Albumin usage in clinical medicine: tradition or therapeutic?". Transfusion Medicine Reviews. 24 (1): 53–63. doi:10.1016/j.tmrv.2009.09.005. PMID 19962575.
  8. ^ "Product Information data sheet" (PDF). Sigma Aldrich.
  9. ^ Mihara E, Hirai H, Yamamoto H, Tamura-Kawakami K, Matano M, Kikuchi A, et al. (February 2016). "Active and water-soluble form of lipidated Wnt protein is maintained by a serum glycoprotein afamin/α-albumin". eLife. 5. doi:10.7554/eLife.11621. PMC 4775226. PMID 26902720.
  10. ^ Nishio H, Heiskanen M, Palotie A, Bélanger L, Dugaiczyk A (May 1996). "Tandem arrangement of the human serum albumin multigene family in the sub-centromeric region of 4q: evolution and chromosomal direction of transcription". Journal of Molecular Biology. 259 (1): 113–9. doi:10.1006/jmbi.1996.0306. PMID 8648639.
  11. ^ Shewry PR, Pandya MJ (1999). "The 2S Albumin Storage Proteins". Seed Proteins. Springer Netherlands. pp. 563–586. doi:10.1007/978-94-011-4431-5_24. ISBN 978-94-011-4431-5.
  12. ^ Peppin L, McEwing R, Webster S, Rogers A, Nicholls D, Ogden R (September 2008). "Development of a field test for the detection of illegal bear products" (PDF). Endangered Species Research. 9 (3): 263–70. doi:10.3354/esr00131.
  13. ^ Bostock J. "Pliny the Elder, The Natural History". Historia Naturalis 28, 6, 18.

External links edit

 
Wikisource has the text of the 1911 Encyclopædia Britannica article "Albumin".
  • Albumins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • The Albumin website
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Serum albumin.

January 01, 1970
albumin, this, article, about, class, proteins, substance, sometimes, called, albumen, white, specific, albumins, found, vertebrate, bloodstreams, serum, albumin, other, uses, disambiguation, this, article, multiple, issues, please, help, improve, discuss, the. This article is about the class of proteins For the substance sometimes called albumen see egg white For the specific albumins found in vertebrate bloodstreams see serum albumin For other uses see Albumin disambiguation This article has multiple issues Please help improve it or discuss these issues on the talk page Learn how and when to remove these template messages This article may require cleanup to meet Wikipedia s quality standards The specific problem is Improved diagram in structure section needed Please help improve this article if you can November 2016 Learn how and when to remove this template message This article needs additional citations for verification Please help improve this article by adding citations to reliable sources Unsourced material may be challenged and removed Find sources Albumin news newspapers books scholar JSTOR March 2009 Learn how and when to remove this template message Learn how and when to remove this template message Albumin is a family of globular proteins the most common of which are the serum albumins All of the proteins of the albumin family are water soluble moderately soluble in concentrated salt solutions and experience heat denaturation Albumins are commonly found in blood plasma and differ from other blood proteins in that they are not glycosylated Substances containing albumins are called albuminoids Serum albumin familyStructure of serum albumin 1 2 IdentifiersSymbolSerum albuminPfamPF00273Pfam clanCL0282InterProIPR014760SMARTSM00103PROSITEPS51438SCOP21ao6 SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB1ao6 1bj5 1bke 1bm0 1e78 1e7a 1e7b 1e7c 1e7e 1e7f 1e7g 1e7h 1e7i 1gni 1gnj 1h9z 1ha2 1hk1 1hk2 1hk3 1hk4 1hk5 1j78 1j7e 1kw2 1kxp 1lot 1ma9 1n5u 1o9x 1tf0 1uor 1ysx 2bx8 2bxa 2bxb 2bxc 2bxd 2bxe 2bxf 2bxg 2bxh 2bxi 2bxk 2bxl 2bxm 2bxn 2bxo 2bxp 2bxq 2i2z 2i30 2vdb 2vue 2vuf 3b9l 3b9m A number of blood transport proteins are evolutionarily related in the albumin family including serum albumin alpha fetoprotein vitamin D binding protein and afamin 3 4 5 This family is only found in vertebrates 6 Albumins in a less strict sense can mean other proteins that coagulate under certain conditions See Other albumin types for lactalbumin ovalbumin and plant 2S albumin Contents 1 Function 2 Classification 2 1 Other albumin types 3 Structure 4 Forensic uses 5 Terminology 6 See also 7 References 8 External linksFunction editAlbumins in general are transport proteins that bind to various ligands and carry them around 6 Human types include Human serum albumin is the main protein of human blood plasma It makes up around 50 of human plasma proteins It binds water cations such as Ca2 Na and K fatty acids hormones bilirubin thyroxine T4 and pharmaceuticals including barbiturates Its main function is to regulate the oncotic pressure of blood 7 The isoelectric point of albumin is 4 7 8 Alpha fetoprotein is a fetal plasma protein that binds various cations fatty acids and bilirubin Vitamin D binding protein binds to vitamin D and its metabolites as well as to fatty acids Not much is known about afamin It seems to carry lipidated Wnt proteins and Vitamin E around 9 Extracellular matrix protein 1 is a less canonical albumin It regulates bone mineralization The four canonical human albumins are arranged on chromosome 4 region 4q13 3 in a tandem manner 10 Classification editAlbumins found in animals can be divided into six subfamilies by phylogeny The Vitamin D binding proteins occupy families 1 3 The other albumins are mixed among each other in families 4 6 ECM1 is in family 6 6 In addition to their medical use serum albumins are valued in biotechnology Bovine serum albumin is usually used although versions from humans and genetically modified rice are also used to reduce animal cruelty Other albumin types edit A few other proteins are also sometimes called albumins They are not in the same family as vertebrate albumins Ovalbumin is a storage protein in egg white albumen It is a serpin Lactalbumin or whey protein is a protein fraction of milk It is mainly Beta lactoglobulin although serum albumin also comprises a small part of it Some plant seeds including hemp encode 2S albumins These are named for their egg like coagulation property 11 Structure editThe 3D structure of human serum albumin has been determined by X ray crystallography to a resolution of 2 5 angstroms 250 pm 1 Albumin is a 65 70 kDa protein Albumin comprises three homologous domains that assemble to form a heart shaped protein 2 Each domain is a product of two subdomains that possess common structural motifs 2 The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA which exhibit similar chemistry Structurally the serum albumins are similar each domain containing five or six internal disulfide bonds Forensic uses editWorldwide certain traditional Chinese medicines contain wild bear bile banned under CITES legislation Dip sticks similar to common pregnancy tests have been developed to detect the presence of bear albumin in traditional medicine products indicating that bear bile had been used in their creation 12 Terminology editAlbumin is pronounced ˈ ae l b j ʊ m ɪ n formed from Latin albumen 13 egg white dried egg white See also editCohn process human serum albumin purification method Serum albumin Bovine serum albumin Human serum albuminReferences editThis article incorporates text from the public domain Pfam and InterPro IPR014760 a b Sugio S Kashima A Mochizuki S Noda M Kobayashi K June 1999 Crystal structure of human serum albumin at 2 5 A resolution Protein Engineering 12 6 439 46 doi 10 1093 protein 12 6 439 PMID 10388840 a b c He XM Carter DC July 1992 Atomic structure and chemistry of human serum albumin Nature 358 6383 209 15 Bibcode 1992Natur 358 209H doi 10 1038 358209a0 PMID 1630489 S2CID 4353741 Haefliger DN Moskaitis JE Schoenberg DR Wahli W October 1989 Amphibian albumins as members of the albumin alpha fetoprotein vitamin D binding protein multigene family Journal of Molecular Evolution 29 4 344 54 Bibcode 1989JMolE 29 344H doi 10 1007 BF02103621 PMID 2481749 S2CID 1456034 Schoentgen F Metz Boutigue MH Jolles J Constans J Jolles P June 1986 Complete amino acid sequence of human vitamin D binding protein group specific component evidence of a three fold internal homology as in serum albumin and alpha fetoprotein Biochimica et Biophysica Acta BBA Protein Structure and Molecular Enzymology 871 2 189 98 doi 10 1016 0167 4838 86 90173 1 PMID 2423133 Lichenstein HS Lyons DE Wurfel MM Johnson DA McGinley MD Leidli JC et al July 1994 Afamin is a new member of the albumin alpha fetoprotein and vitamin D binding protein gene family The Journal of Biological Chemistry 269 27 18149 54 doi 10 1016 S0021 9258 17 32429 8 PMID 7517938 a b c Li S Cao Y Geng F 2017 Genome Wide Identification and Comparative Analysis of Albumin Family in Vertebrates Evolutionary Bioinformatics Online 13 1176934317716089 doi 10 1177 1176934317716089 PMC 5480655 PMID 28680266 Farrugia A January 2010 Albumin usage in clinical medicine tradition or therapeutic Transfusion Medicine Reviews 24 1 53 63 doi 10 1016 j tmrv 2009 09 005 PMID 19962575 Product Information data sheet PDF Sigma Aldrich Mihara E Hirai H Yamamoto H Tamura Kawakami K Matano M Kikuchi A et al February 2016 Active and water soluble form of lipidated Wnt protein is maintained by a serum glycoprotein afamin a albumin eLife 5 doi 10 7554 eLife 11621 PMC 4775226 PMID 26902720 Nishio H Heiskanen M Palotie A Belanger L Dugaiczyk A May 1996 Tandem arrangement of the human serum albumin multigene family in the sub centromeric region of 4q evolution and chromosomal direction of transcription Journal of Molecular Biology 259 1 113 9 doi 10 1006 jmbi 1996 0306 PMID 8648639 Shewry PR Pandya MJ 1999 The 2S Albumin Storage Proteins Seed Proteins Springer Netherlands pp 563 586 doi 10 1007 978 94 011 4431 5 24 ISBN 978 94 011 4431 5 Peppin L McEwing R Webster S Rogers A Nicholls D Ogden R September 2008 Development of a field test for the detection of illegal bear products PDF Endangered Species Research 9 3 263 70 doi 10 3354 esr00131 Bostock J Pliny the Elder The Natural History Historia Naturalis 28 6 18 External links edit nbsp Wikisource has the text of the 1911 Encyclopaedia Britannica article Albumin Albumins at the U S National Library of Medicine Medical Subject Headings MeSH The Albumin website Albumin binding prediction PDBe KB provides an overview of all the structure information available in the PDB for Human Serum albumin Retrieved from https en wikipedia org w index php title Albumin amp oldid 1182518857, wikipedia, wiki, book, books, library,

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