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'''Albumin''' is a [[protein family|family]] of [[globular protein]]s, the most common of which are the [[serum albumin]]s. All the proteins of the albumin family are water-[[solubility|soluble]], moderately soluble in concentrated salt solutions, and experience heat [[denaturation (biochemistry)|denaturation]]. Albumins are commonly found in [[blood plasma]] and differ from other [[blood proteins]] in that they are not [[glycosylation|glycosylated]]. Substances containing albumins, such as [[egg white]], are called ''albuminoids''.
'''Albumin''' is a [[protein family|family]] of [[globular protein]]s, the most common of which are the [[serum albumin]]s. All the proteins of the albumin family are water-[[solubility|soluble]], moderately soluble in concentrated salt solutions, and experience heat [[denaturation (biochemistry)|denaturation]]. Albumins are commonly found in [[blood plasma]] and differ from other [[blood proteins]] in that they are not [[glycosylation|glycosylated]]. Substances containing albumins, such as [[egg white]], are called ''albuminoids''.


A number of blood [[transport protein]]s are evolutionarily related, including serum albumin, [[alpha-fetoprotein]], [[vitamin D-binding protein]] and [[afamin]].<ref name="pmid2481749">{{cite journal|last1=Haefliger|first1=Denise Nardelli|last2=Moskaitis|first2=John E.|last3=Schoenberg|first3=Daniel R.|last4=Wahli|first4=Walter|title=Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family|journal=Journal of Molecular Evolution|date=October 1989|volume=29|issue=4|pages=344–354|pmid = 2481749|doi=10.1007/BF02103621|bibcode=1989JMolE..29..344H}}</ref><ref name="pmid2423133">{{cite journal|last1=Schoentgen|first1=Francçoise|last2=Metz-Boutique|first2=Marie-Hélène|last3=Jollès|first3=Jacqueline|last4=Constans|first4=Jacques|last5=Jollès|first5=Pierre|title=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 α-fetoprotein|journal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|date=June 1986|volume=871|issue=2|pages=189–198| pmid = 2423133|doi=10.1016/0167-4838(86)90173-1}}</ref><ref name="pmid7517938">{{cite journal|last1=Lichenstein|first1=HS|last2=Lyons|first2=DE|last3=Wurfel|first3=MM|last4=Johnson|first4=DA|last5=McGinley|first5=MD|last6=Leidli|first6=JC|last7=Trollinger|first7=DB|last8=Mayer|first8=JP|last9=Wright|first9=SD|last10=Zukowski|first10=MM|title=Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.|journal=The Journal of Biological Chemistry|date=8 July 1994|volume=269|issue=27|pages=18149–54|pmid=7517938}}</ref>
A number of blood [[transport protein]]s are evolutionarily related in the albumin family, including serum albumin, [[alpha-fetoprotein]], [[vitamin D-binding protein]] and [[afamin]].<ref name="pmid2481749">{{cite journal|last1=Haefliger|first1=Denise Nardelli|last2=Moskaitis|first2=John E.|last3=Schoenberg|first3=Daniel R.|last4=Wahli|first4=Walter|title=Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family|journal=Journal of Molecular Evolution|date=October 1989|volume=29|issue=4|pages=344–354|pmid = 2481749|doi=10.1007/BF02103621|bibcode=1989JMolE..29..344H}}</ref><ref name="pmid2423133">{{cite journal|last1=Schoentgen|first1=Francçoise|last2=Metz-Boutique|first2=Marie-Hélène|last3=Jollès|first3=Jacqueline|last4=Constans|first4=Jacques|last5=Jollès|first5=Pierre|title=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 α-fetoprotein|journal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|date=June 1986|volume=871|issue=2|pages=189–198| pmid = 2423133|doi=10.1016/0167-4838(86)90173-1}}</ref><ref name="pmid7517938">{{cite journal|last1=Lichenstein|first1=HS|last2=Lyons|first2=DE|last3=Wurfel|first3=MM|last4=Johnson|first4=DA|last5=McGinley|first5=MD|last6=Leidli|first6=JC|last7=Trollinger|first7=DB|last8=Mayer|first8=JP|last9=Wright|first9=SD|last10=Zukowski|first10=MM|title=Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.|journal=The Journal of Biological Chemistry|date=8 July 1994|volume=269|issue=27|pages=18149–54|pmid=7517938}}</ref> This family is only found in [[vertebrates]].<ref name="pmid28680266">{{cite journal |last1=Li |first1=S |last2=Cao |first2=Y |last3=Geng |first3=F |title=Genome-Wide Identification and Comparative Analysis of Albumin Family in Vertebrates. |journal=Evolutionary bioinformatics online |date=2017 |volume=13 |pages=1176934317716089 |doi=10.1177/1176934317716089 |pmid=28680266 |pmc=5480655}}</ref>


Albumin binds to the cell surface receptor [[albondin]].
Serum albumin binds to the cell surface receptor [[albondin]].


== Function ==
== Function ==
Albumins in general are [[transport protein]]s that bind to various [[ligand]]s and carry them around.<ref name="pmid28680266"/> Human types include:
Serum albumin is the main protein of human blood plasma.<ref name=Farrugia2010>{{cite journal|last1=Farrugia|first1=Albert|title=Albumin Usage in Clinical Medicine: Tradition or Therapeutic?|journal=Transfusion Medicine Reviews|date=January 2010|volume=24|issue=1|pages=53–63|pmid=19962575|doi=10.1016/j.tmrv.2009.09.005}}</ref> It binds water, cations (such as Ca<sup>2+</sup>, Na<sup>+</sup> and K<sup>+</sup>), [[fatty acid]]s, hormones, [[bilirubin]], thyroxine (T4) and pharmaceuticals (including barbiturates): its main function is to regulate the [[oncotic pressure]] of blood. [[Alpha-fetoprotein]] (alpha-fetoglobulin) 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. The [[isoelectric point]] of albumin is 4.9.
* 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 Ca<sup>2+</sup>, Na<sup>+</sup> and K<sup>+</sup>), [[fatty acid]]s, hormones, [[bilirubin]], thyroxine (T4) and pharmaceuticals (including barbiturates). Its main function is to regulate the [[oncotic pressure]] of blood.<ref name=Farrugia2010>{{cite journal|last1=Farrugia|first1=Albert|title=Albumin Usage in Clinical Medicine: Tradition or Therapeutic?|journal=Transfusion Medicine Reviews|date=January 2010|volume=24|issue=1|pages=53–63|pmid=19962575|doi=10.1016/j.tmrv.2009.09.005}}</ref> The [[isoelectric point]] of albumin is 4.9.
* [[Alpha-fetoprotein]] (alpha-fetoglobulin) 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 protein]]s and Vitamin E around.<ref>{{cite journal |last1=Mihara |first1=E |last2=Hirai |first2=H |last3=Yamamoto |first3=H |last4=Tamura-Kawakami |first4=K |last5=Matano |first5=M |last6=Kikuchi |first6=A |last7=Sato |first7=T |last8=Takagi |first8=J |title=Active and water-soluble form of lipidated Wnt protein is maintained by a serum glycoprotein afamin/α-albumin. |journal=eLife |date=23 February 2016 |volume=5 |doi=10.7554/eLife.11621 |pmid=26902720}}</ref>
* [[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.<ref>{{cite journal |last1=Nishio |first1=H |last2=Heiskanen |first2=M |last3=Palotie |first3=A |last4=Bélanger |first4=L |last5=Dugaiczyk |first5=A |title=Tandem arrangement of the human serum albumin multigene family in the sub-centromeric region of 4q: evolution and chromosomal direction of transcription. |journal=Journal of molecular biology |date=31 May 1996 |volume=259 |issue=1 |pages=113-9 |doi=10.1006/jmbi.1996.0306 |pmid=8648639}}</ref>
== Medical uses ==
For people with low blood volume, there is no evidence that albumin reduces mortality when compared with cheaper alternatives such as [[normal saline]], or that albumin reduces mortality in patients with burns and low albumin levels. Therefore, the [[Cochrane Collaboration]] recommends that it should not be used, except in [[clinical trials]].<ref name="Coc11">{{cite journal|date=9 November 2011|title=Human albumin solution for resuscitation and volume expansion in critically ill patients.|url=|journal=The Cochrane Database of Systematic Reviews|volume=|issue=11|page=CD001208|doi=10.1002/14651858.CD001208.pub4|pmid=22071799|vauthors=Roberts I, Blackhall K, Alderson P, Bunn F, Schierhout G|pmc=7055200}}</ref>{{Update inline|reason=Updated version https://www.ncbi.nlm.nih.gov/pubmed/22071799|date=December 2016}}


== Classification ==
In [[acoustic droplet vaporization]] (ADV), albumin is sometimes used as a [[surfactant]]. ADV has been proposed as a cancer treatment by means of [[occlusion therapy]].<ref>{{cite journal|last1=Lo|first1=Andrea|last2=Kripfgans|first2=Oliver|last3=Carson|first3=Paul|last4=Rothman|first4=Edward|last5=Fowlkes|first5=J.|title=Acoustic droplet vaporization threshold: effects of pulse duration and contrast agent|journal=IEEE Transactions on Ultrasonics, Ferroelectrics and Frequency Control|date=May 2007|volume=54|issue=5|pages=933–946|doi=10.1109/tuffc.2007.339|pmid=17523558}}</ref>
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.<ref name="pmid28680266"/>


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#Production_of_recombinant_proteins|genetically-modified rice]] are also used to reduce animal cruelty.
Human serum albumin may be used to potentially reverse drug/chemical toxicity by binding to free drug/agent.<ref>{{Cite journal|last=Ascenzi|first=Paolo|last2=Leboffe|first2=Loris|last3=Toti|first3=Daniele|last4=Polticelli|first4=Fabio|last5=Trezza|first5=Viviana|date=2018-04-15|title=Fipronil recognition by the FA1 site of human serum albumin|journal=Journal of Molecular Recognition|language=en|volume=31|issue=8|pages=e2713|doi=10.1002/jmr.2713|pmid=29656610|issn=0952-3499}}</ref>


⚫
=== Other albumin types ===
Human albumin may also be used in treatment of decompensated cirrhosis.<ref>{{Cite journal|last=Paolo|first=Caraceni|date=31 May 2018|title=Long-term albumin administration in decompensated cirrhosis (ANSWER): an open-label randomised trial|doi=10.1016/S0140-6736(18)30840-7|pmid=29861076|journal=The Lancet|volume=391|issue=10138|pages=2417–2429|hdl=2108/208667|hdl-access=free}}</ref>

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]].
* Some plant [[seed]]s, including [[hemp protein|hemp]], encode "albumins". These are named for their egg-like coagulation property.<ref>{{cite book |last1=Shewry |first1=Peter R. |last2=Pandya |first2=Maya J. |title=Seed Proteins |publisher=Springer Netherlands |isbn=978-94-011-4431-5 |chapter=The 2S Albumin Storage Proteins |doi=10.1007/978-94-011-4431-5_24}}</ref>


== Structure ==
== Structure ==
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Albumin comprises three homologous domains that assemble to form a heart-shaped protein.<ref name="pmid1630489"/> Each domain is a product of two subdomains that possess common structural motifs.<ref name="pmid1630489"/> 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.
Albumin comprises three homologous domains that assemble to form a heart-shaped protein.<ref name="pmid1630489"/> Each domain is a product of two subdomains that possess common structural motifs.<ref name="pmid1630489"/> 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.

== Serum albumin ==
{{main|Serum albumin}}
Serum albumin is the most abundant [[blood plasma]] protein and is produced in the [[liver]] and forms a large proportion of all plasma protein. The human version is [[human serum albumin]], and it normally constitutes about 50% of [[human]] plasma protein.<ref name=Farrugia2010/>

Serum albumins are important in regulating blood volume by maintaining the [[oncotic pressure]] (also known as [[colloid osmotic pressure]]) of the blood compartment.<ref name=Farrugia2010/> They also serve as carriers for molecules of low water solubility this way isolating their hydrophobic nature, including lipid-soluble hormones, [[bile]] salts, [[unconjugated bilirubin]], free [[fatty acid]]s ([[Apolipoprotein|apoprotein]]), [[calcium]], ions ([[transferrin]]), and some drugs like warfarin, phenobutazone, clofibrate & phenytoin. For this reason, it is sometimes referred as a molecular "taxi". Competition between drugs for albumin binding sites may cause drug interaction by increasing the free fraction of one of the drugs, thereby affecting potency.

Specific types include:
* [[human serum albumin]]
* [[bovine serum albumin]] (cattle serum albumin) or BSA, often used in medical and molecular biology labs.

=== Serum albumin levels ===

The normal range of human serum albumin in adults (> 3 y.o.) is 3.5 to 5 g/dL. For children less than three years of age, the normal range is broader, 2.9–5.5 g/dL.<ref>{{cite web|url=http://www.rush.edu/webapps/rml/RMLRangesCMP.jsp |title=Normal Ranges for Common Laboratory Tests. |accessdate=2007-12-06 |url-status=bot: unknown |archiveurl=https://web.archive.org/web/20130114222140/http://www.rush.edu/webapps/rml/RMLRangesCMP.jsp |archivedate=2013-01-14 }} [[Rush University]]</ref>

Low albumin ([[hypoalbuminemia]]) may be caused by [[liver disease]], [[nephrotic syndrome]], burns, [[protein-losing enteropathy]], [[malabsorption]], [[malnutrition]], late pregnancy, artefact, genetic variations and malignancy.

High albumin ([[hyperalbuminemia]]) is almost always caused by dehydration. In some cases of [[retinol]] ([[Vitamin A]]) deficiency, the albumin level can be elevated to high-normal values (e.g., 4.9 g/dL). This is because retinol causes cells to swell with water (this is also the reason too much Vitamin A is toxic).<ref>{{cite journal|last1=Pasantes-Morales|first1=H|last2=Wright|first2=CE|last3=Gaull|first3=GE|title=Protective effect of taurine, zinc and tocopherol on retinol-induced damage in human lymphoblastoid cells.|journal=The Journal of Nutrition|date=December 1984|volume=114|issue=12|pages=2256–61|pmid=6502269|doi=10.1093/jn/114.12.2256}}</ref>
This swelling also likely occurs during treatment with 13-cis retinoic acid ([[Isotretinoin|isotretnoin]]), a pharmaceutical for treating severe acne, amongst other conditions. In lab experiments it has been shown that all-trans retinoic acid down regulates human albumin production.<ref>{{cite journal |last1=Masaki |first1=T |last2=Matsuura |first2=T |last3=Ohkawa |first3=K|last4=Miyamura|first4=T|last5=Okazaki|first5=I|last6=Watanabe|first6=T|last7=Suzuki|first7=T|title=All-trans retinoic acid down-regulates human albumin gene expression through the induction of C/EBPbeta-LIP.|journal=The Biochemical Journal|date=15 July 2006 |volume=397 |issue=2 |pages=345–53 |pmid=16608438|doi=10.1042/BJ20051863|pmc=1513275}}</ref>

⚫
=== Other albumin types ===

Other albumin types include the [[storage protein]] [[ovalbumin]] in egg white, and different storage albumins in the [[seed]]s of some [[plant]]s, including [[hemp protein|hemp]].<ref name="High Times">{{cite news|url=http://www.hightimes.com/read/hemp-repairs-damaged-dna|title=Hemp Repairs Damaged DNA|publisher=[[High Times]]|accessdate= 10 Sep 2014|date=28 Aug 2014}}</ref>
* Note that the protein "albumin" is spelled with an "i", while "albumen" with an "e", is the white of an egg, which contains (among other things) several dozen types of albumin (with an "i"), mostly [[ovalbumin]].


==Forensic uses==
==Forensic uses==

Revision as of 13:57, 19 April 2020

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).
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​

Albumin is a family of globular proteins, the most common of which are the serum albumins. All 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, such as egg white, are called albuminoids.

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]

Serum albumin binds to the cell surface receptor albondin.

Function

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

  • 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 4.9.
  • Alpha-fetoprotein (alpha-fetoglobulin) 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.[8]
  • 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.[9]

Classification

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

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

Structure

The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 ångströms (250 pm).[11] 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

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

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

See also

References

This article incorporates text from the public domain Pfam and InterPro: IPR014760
  1. ^ Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. (1 June 1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering Design and Selection. 12 (6): 439–446. doi:10.1093/protein/12.6.439. PMID 10388840.
  2. ^ a b c He, Xiao Min; Carter, Daniel C. (16 July 1992). "Atomic structure and chemistry of human serum albumin". Nature. 358 (6383): 209–215. Bibcode:1992Natur.358..209H. doi:10.1038/358209a0. PMID 1630489.
  3. ^ Haefliger, Denise Nardelli; Moskaitis, John E.; Schoenberg, Daniel R.; Wahli, Walter (October 1989). "Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family". Journal of Molecular Evolution. 29 (4): 344–354. Bibcode:1989JMolE..29..344H. doi:10.1007/BF02103621. PMID 2481749.
  4. ^ Schoentgen, Francçoise; Metz-Boutique, Marie-Hélène; Jollès, Jacqueline; Constans, Jacques; Jollès, Pierre (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 α-fetoprotein". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 871 (2): 189–198. doi:10.1016/0167-4838(86)90173-1. PMID 2423133.
  5. ^ Lichenstein, HS; Lyons, DE; Wurfel, MM; Johnson, DA; McGinley, MD; Leidli, JC; Trollinger, DB; Mayer, JP; Wright, SD; Zukowski, MM (8 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. 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, Albert (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. ^ Mihara, E; Hirai, H; Yamamoto, H; Tamura-Kawakami, K; Matano, M; Kikuchi, A; Sato, T; Takagi, J (23 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. PMID 26902720.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  9. ^ Nishio, H; Heiskanen, M; Palotie, A; Bélanger, L; Dugaiczyk, A (31 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.
  10. ^ Shewry, Peter R.; Pandya, Maya J. "The 2S Albumin Storage Proteins". Seed Proteins. Springer Netherlands. doi:10.1007/978-94-011-4431-5_24. ISBN 978-94-011-4431-5.
  11. ^ Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. (1 June 1999). "Crystal structure of human serum albumin at 2.5 A resolution". Protein Engineering Design and Selection. 12 (6): 439–446. doi:10.1093/protein/12.6.439. PMID 10388840.
  12. ^ Peppin, McEwing, Webster, Rogers, Nicholls, Ogden 2008 'Development of a field test for the detection of illegal bear products' Endangered Forensics Research (9) https://www.int-res.com/articles/esr2009/9/n009p263.pdf
  13. ^ Pliny The Elder. Historia Naturalis 28, 6, 18.

External links

Wikisource has the text of the 1911 Encyclopædia Britannica article "Albumin".
Retrieved from "https://en.wikipedia.org/w/index.php?title=Albumin&oldid=951900939"