Mutations and polymorphisms of the gene of the major human blood protein, serum albumin

We have tabulated the 77 currently known mutations of the familiar human blood protein, serum albumin
(ALB). A total of 65 mutations result in bisalbuminemia. Physiological and structural effects of these mutations
are included where observed. Most of the changes are benign. The majority of them were detected upon clinical
electrophoretic studies, as a result of a point mutation of a charged amino acid residue. Three were discovered
by their strong binding of thyroxine or triiodothyronine. A total of 12 of the tabulated mutations result in
analbuminemia, defined as a serum albumin concentration of <1 g/L. These were generally detected upon
finding a low albumin concentration in patients with mild edema, and involve either splicing errors negating
translation or premature stop codons producing truncated albumin molecules. A total of nine mutations, five of
those with analbuminemia and four resulting in variants modified near the C-terminal end, cause frameshifts.
Allotypes from three of the point mutations become N-glycosylated and one C-terminal frameshift mutation
shows O-glycosylation.