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. Structure The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure. 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. Types Serum albumin is widely distributed in mammals. 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 (including venom toxicity), and molecular biology laboratories (usually to leverage its non-specific protein binding properties). See also Blood plasma fractionation Bovine serum albumin Chromatography in blood processing Human serum albumin Lactalbumin Ovalbumin References External links RCSB Protein Data Bank : Molecule of the Month – Serum Albumin Albumin binding prediction Blood proteins