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OMIM@xiajingbo:103600-35-ALB JSONTXT

In albumin Casebrook, an electrophoretically slow albumin variant with a relative molecular mass of 2.5 kD higher than normal albumin, Peach and Brennan (1991) identified substitution of asparagine for aspartic acid-494. The mutation introduced an asn-glu-thr N-linked oligosaccharide attachment sequence centered on asn494, which explained the increase in molecular mass. The mutant albumin was associated with no apparent pathology and was detected in 2 unrelated individuals of Anglo-Saxon descent.

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