Serum albumin: Difference between revisions
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==General characteristics== |
==General characteristics== |
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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. |
Albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. The [[glomerular basement membrane]] is also negatively charged in the body; 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. |
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Because smaller animals (for example [[rat]]s) function at a lower [[blood pressure]], they need less [[oncotic pressure]] to balance this, and thus need less albumin to maintain proper fluid distribution. |
Because smaller animals (for example [[rat]]s) function at a lower [[blood pressure]], they need less [[oncotic pressure]] to balance this, and thus need less albumin to maintain proper fluid distribution. |
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Revision as of 00:20, 16 April 2008
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.
Types
- 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 (usually to leverage its non-specific protein binding properties).
General characteristics
Albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. The glomerular basement membrane is also negatively charged in the body; 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].