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 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. This family is only found in vertebrates.
Background References
1. "Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures." Bhattacharya A.A., Curry S., Franks N.P. J. Biol. Chem. 275:38731-38738(2000)
2. "Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids." Petitpas I., Grune T., Bhattacharya A.A., Curry S. J. Mol. Biol. 314:955-960(2001)
3. "A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges." Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., Pucci P., Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., Galliano M. Eur. J. Biochem. 268:344-352(2001)
Sequence Similarity
Belongs to the ALB/AFP/VDB family.
Tissue Specificity
Plasma.
Post-translational Modification
Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.; Glycated in diabetic patients.; Phosphorylated by FAM20C in the extracellular medium.; Acetylated on Lys-223 by acetylsalicylic acid.