Genetic variants showing apparent hot-spots in the human serum albumin gene.
The molecular defects of three different slow-migrating genetic variants of human serum albumin, albumins Kamloops (formerly RIH), Stirling and Amsterdam, previously characterized only by electrophoretic and dye-binding studies, are now reported. Two of them are proalbumin variants: sequential analysis of the purified whole proteins has established the mutation responsible for albumin Kamloops as -1Arg-->Gln, and for albumin Stirling as -2Arg-->His. A Glu-->Lys substitution in position 570 of the mature albumin molecule was determined in albumin Amsterdam by sequential analysis of two abnormal tryptic fragments. The three alloalbumins are caused by single-base changes all of which seem to represent hot-spots in the albumin gene. The possible functional consequences of the presence of a circulating alloalbumin are discussed.
Galliano
M
M
Department of Biochemistry, University of Pavia, I-27100, Pavia, Italy.
Kragh-Hansen
U
U
Tárnoky
A L
AL
Chapman
J C
JC
Campagnoli
M
M
Minchiotti
L
L
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D014644:Genetic Variation; D006579:Heterozygote; D006801:Humans; D009154:Mutation; D012709:Serum Albumin / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000302:isolation & purification; D000075462:Serum Albumin, Human
D012709:Serum Albumin; C402606:albumin Amsterdam; C402604:albumin Kamloops; C402605:albumin Stirling; D000075462:Serum Albumin, Human