Serum albumin

Serum albumin, often referred to simply as blood albumin, is an

albumin (a type of globular protein) found in vertebrate blood.
Serum albumin family
Human serum albumin is encoded by the ALB gene.[2][3][4] Other
mammalian forms, such as bovine serum albumin, are chemically
similar.

Serum albumin is produced by the liver, occurs dissolved in blood

plasma and is the most abundant blood protein in mammals.
Albumin is essential for maintaining the oncotic pressure needed for
proper distribution of body fluids between blood vessels and body
tissues; without albumin, the high pressure in the blood vessels
would force more fluids out into the tissues. It also acts as a plasma Structure of human serum albumin.[1]
carrier by non-specifically binding several hydrophobic steroid Identifiers
hormones and as a transport protein for hemin and fatty acids. Too Symbol Serum_albumin
much or too little circulating serum albumin may be harmful.
Albumin in the urine usually denotes the presence of kidney Pfam PF00273 (http://pfam.xfa
disease. Occasionally albumin appears in the urine of normal m.org/family?acc=PF0027
persons following long periods of standing (postural albuminuria). 3)
Pfam CL0282 (http://pfam.xfam.
clan org/clan/CL0282)
Contents InterPro IPR014760 (https://www.e
bi.ac.uk/interpro/entry/IPR
Function
014760)
Synthesis
SMART SM00103 (http://smart.em
Properties
bl-heidelberg.de/smart/do
Structure _annotation.pl?DOMAIN=
Types SM00103)
See also PROSITE PS51438 (http://www.expa
References sy.org/cgi-bin/prosite-sear
ch-ac?PS51438)
External links
SCOPe 1ao6 (https://scop.berkele
y.edu/search/key=1ao6) /
Function SUPFAM (http://supfam.or
g/SUPERFAMILY/cgi-bin/s
Albumin functions primarily as a carrier protein for steroids, fatty earch.cgi?search_field=1a
acids, and thyroid hormones in the blood and plays a major role in o6)
stabilizing extracellular fluid volume by contributing to oncotic Available protein structures:
pressure (known also as colloid osmotic pressure) of plasma.
Pfam structures (http://pfam.xfam.or
Because smaller animals (for example rats) function at a lower g/family/PF00273?tab=pdbBlo
blood pressure, they need less oncotic pressure to balance this, and ck) / ECOD (http://prodata.swm
ed.edu/ecod/complete/searc
thus need less albumin to maintain proper fluid distribution.
h?kw=PF00273)

PDB RCSB PDB (http://www.rcsb.or

 g/pdb/search/smartSubquery.d
Synthesis o?smartSearchSubtype=PfamI
dQuery&pfamID=PF00273);
Albumin is synthesized in the liver as preproalbumin which has an PDBe (https://www.ebi.ac.uk/p
N-terminal peptide that is removed before the nascent protein is dbe/entry/search/index?pfam_
released from the rough endoplasmic reticulum. The product, accession:PF00273); PDBj (htt
proalbumin, is in turn cleaved in the Golgi vesicles to produce the ps://pdbj.org/searchFor?query
secreted albumin.[4] =PF00273)

PDBsum structure summary (https://ww

Properties w.ebi.ac.uk/thornton-srv/datab
ases/cgi-bin/pdbsum/GetPfam
Str.pl?pfam_id=PF00273)
Albumin is a globular, water-soluble, un-glycosylated serum protein
PDB 1ao6 (https://www.rcsb.org/stru
of approximate molecular weight of 65,000 Daltons.
cture/1ao6), 1bj5 (https://www.r
Albumin (when ionized in water at pH 7.4, as found in the body) is csb.org/structure/1bj5), 1bke
(https://www.rcsb.org/structure/
negatively charged. The glomerular basement membrane is also
1bke), 1bm0 (https://www.rcsb.
negatively charged in the body; some studies suggest that this
org/structure/1bm0), 1e78 (http
prevents the filtration of albumin in the urine. According to this
s://www.rcsb.org/structure/1e7
theory, that charge plays a major role in the selective exclusion of 8), 1e7a (https://www.rcsb.org/
albumin from the glomerular filtrate. A defect in this property results structure/1e7a), 1e7b (https://w
in nephrotic syndrome leading to albumin loss in the urine. ww.rcsb.org/structure/1e7b),
Nephrotic syndrome patients are sometimes given albumin to 1e7c (https://www.rcsb.org/stru
replace the lost albumin. cture/1e7c), 1e7e (https://www.
rcsb.org/structure/1e7e), 1e7f

Structure (https://www.rcsb.org/structure/
1e7f), 1e7g (https://www.rcsb.o
rg/structure/1e7g), 1e7h (http
The general structure of albumin is characterized by several long α s://www.rcsb.org/structure/1e7
helices allowing it to maintain a relatively static shape, which is h), 1e7i (https://www.rcsb.org/s
essential for regulating blood pressure. tructure/1e7i), 1gni (https://ww
w.rcsb.org/structure/1gni), 1gnj
Serum albumin contains eleven distinct binding domains for (https://www.rcsb.org/structure/
hydrophobic compounds. One hemin and six long-chain fatty acids 1gnj), 1h9z (https://www.rcsb.o
can bind to serum albumin at the same time.[5] rg/structure/1h9z), 1ha2 (http
s://www.rcsb.org/structure/1ha
2), 1hk1 (https://www.rcsb.org/
Types structure/1hk1), 1hk2 (https://w
ww.rcsb.org/structure/1hk2),
Serum albumin is widely distributed in mammals. 1hk3 (https://www.rcsb.org/stru
cture/1hk3), 1hk4 (https://www.
The human version is human serum albumin. rcsb.org/structure/1hk4), 1hk5
Bovine serum albumin, or BSA, is commonly used in (https://www.rcsb.org/structure/
immunodiagnostic procedures, clinical chemistry 1hk5), 1j78 (https://www.rcsb.o
reagents, cell culture media, protein chemistry research rg/structure/1j78), 1j7e (https://
(including venom toxicity), and molecular biology www.rcsb.org/structure/1j7e),
laboratories (usually to leverage its non-specific protein 1kw2 (https://www.rcsb.org/stru
binding properties). cture/1kw2), 1kxp (https://www.
rcsb.org/structure/1kxp), 1lot (h
ttps://www.rcsb.org/structure/1l
See also ot), 1ma9 (https://www.rcsb.or
g/structure/1ma9), 1n5u (http
Human serum albumin s://www.rcsb.org/structure/1n5
Bovine serum albumin u), 1o9x (https://www.rcsb.org/
 Blood plasma fractionation structure/1o9x), 1tf0 (https://ww
w.rcsb.org/structure/1tf0), 1uor
Chromatography in blood processing
(https://www.rcsb.org/structure/
Lactalbumin 1uor), 1ysx (https://www.rcsb.o
Ovalbumin rg/structure/1ysx), 2bx8 (http
s://www.rcsb.org/structure/2bx
8), 2bxa (https://www.rcsb.org/
References structure/2bxa), 2bxb (https://w
ww.rcsb.org/structure/2bxb),
1. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K 2bxc (https://www.rcsb.org/stru
(June 1999). "Crystal structure of human serum albumin cture/2bxc), 2bxd (https://www.
at 2.5 A resolution" (https://doi.org/10.1093/protein/12.6.4 rcsb.org/structure/2bxd), 2bxe
39). Protein Engineering. 12 (6): 439–46. (https://www.rcsb.org/structure/
doi:10.1093/protein/12.6.439 (https://doi.org/10.1093%2F 2bxe), 2bxf (https://www.rcsb.o
protein%2F12.6.439). PMID 10388840 (https://pubmed.n rg/structure/2bxf), 2bxg (https://
cbi.nlm.nih.gov/10388840). www.rcsb.org/structure/2bxg),
2. Hawkins JW, Dugaiczyk A (1982). "The human serum 2bxh (https://www.rcsb.org/stru
albumin gene: structure of a unique locus". Gene. 19 (1): cture/2bxh), 2bxi (https://www.r
55–8. doi:10.1016/0378-1119(82)90188-3 (https://doi.org/ csb.org/structure/2bxi), 2bxk (h
10.1016%2F0378-1119%2882%2990188-3). ttps://www.rcsb.org/structure/2
PMID 6292049 (https://pubmed.ncbi.nlm.nih.gov/629204 bxk), 2bxl (https://www.rcsb.or
9). g/structure/2bxl), 2bxm (https://
3. Harper ME, Dugaiczyk A (July 1983). "Linkage of the www.rcsb.org/structure/2bxm),
evolutionarily-related serum albumin and alpha- 2bxn (https://www.rcsb.org/stru
fetoprotein genes within q11-22 of human chromosome cture/2bxn), 2bxo (https://www.
4" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16857 rcsb.org/structure/2bxo), 2bxp
23). American Journal of Human Genetics. 35 (4): 565– (https://www.rcsb.org/structure/
72. PMC 1685723 (https://www.ncbi.nlm.nih.gov/pmc/arti 2bxp), 2bxq (https://www.rcsb.
cles/PMC1685723). PMID 6192711 (https://pubmed.ncbi. org/structure/2bxq), 2i2z (http
nlm.nih.gov/6192711). s://www.rcsb.org/structure/2i2
4. "Entrez Gene: albumin" (https://www.ncbi.nlm.nih.gov/site z), 2i30 (https://www.rcsb.org/st
s/entrez?Db=gene&Cmd=ShowDetailView&TermToSear ructure/2i30), 2vdb (https://ww
ch=213). w.rcsb.org/structure/2vdb),
2vue (https://www.rcsb.org/stru
5. Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry S
cture/2vue), 2vuf (https://www.r
(July 2003). "Crystal structural analysis of human serum
csb.org/structure/2vuf), 3b9l (ht
albumin complexed with hemin and fatty acid" (https://ww
tps://www.rcsb.org/structure/3b
w.ncbi.nlm.nih.gov/pmc/articles/PMC166163). BMC
9l), 3b9m (https://www.rcsb.or
Structural Biology. 3: 6. doi:10.1186/1472-6807-3-6 (http
g/structure/3b9m)
s://doi.org/10.1186%2F1472-6807-3-6). PMC 166163 (htt
ps://www.ncbi.nlm.nih.gov/pmc/articles/PMC166163).
PMID 12846933 (https://pubmed.ncbi.nlm.nih.gov/12846933).

External links
RCSB Protein Data Bank : Molecule of the Month – Serum Albumin (http://www.pdb.org/pdb/sta
tic.do?p=education_discussion/molecule_of_the_month/pdb37_1.html)
Albumin binding prediction (http://albumin.althotas.com/)
Overview of all the structural information available in the PDB for UniProt: P02768 (https://www.
ebi.ac.uk/pdbe/pdbe-kb/proteins/P02768) (Human Serum albumin) at the PDBe-KB.

Retrieved from "https://en.wikipedia.org/w/index.php?title=Serum_albumin&oldid=964043022"

This page was last edited on 23 June 2020, at 08:05 (UTC).

Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this
site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia
Foundation, Inc., a non-profit organization.