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Serum albumin

Serum albumin, often referred to simply as albumin, is the most abundant plasma protein in humans and other mammals. Albumin is essential for maintaining the osmotic pressure needed for proper distribution of body fluids between intravascular compartments and body tissues. It also acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids.


  • The human version is human serum albumin.
  • Bovine serum albumin, or BSA, is commonly used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research and molecular biology laboratories.

General characteristics

Albumin is negatively charged. The glomerular basement membrane is also negatively charged; some studies suggest that this prevents the filtration of albumin in the urine. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. A defect in this property results in nephrotic syndrome leading to albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.

Because smaller animals (for example rats) function at a lower blood pressure, they need less oncotic pressure to balance this, and thus need less albumin to maintain proper fluid distribution.

Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time [1].


  1. ^ BMC Structural Biology 2003, 3(1):6 2003. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. Zunszain, Patricia A Ghuman, Jamie Komatsu, Teruyuki Tsuchida, Eishun Curry, Stephen doi: 10.1186/1472-6807-3-6 PMID 12846933 online
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Serum_albumin". A list of authors is available in Wikipedia.
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