Identification of two apolipoprotein variants, A-I Karatsu (Tyr 100-->His) and A-I Kurume (His 162-->Gln).
We identified two apolipoprotein (apo) A-I variants, using isoelectric focusing gel electrophoresis: apo A-I Karatsu, which had a relative charge of +1 compared to normal apo A-I4, and apo A-I Kurume, which had a relative charge of -1. Direct sequence analysis of the PCR-amplified DNA from the proband of apo A-I Karatsu revealed a single substitution of tyrosine (TAC) for histidine (CAC) at position 100. Sequence analysis of apo A-I Kurume revealed a single substitution of histidine (CAT) for glutamine (CAG) at position 162. Probands of these two mutants and limited family study showed no accelerated atherosclerosis.
Moriyama
K
K
Department of Internal Medicine, Fukuoka University, School of Medicine, Japan.
Sasaki
J
J
Matsunaga
A
A
Takada
Y
Y
Kagimoto
M
M
Arakawa
K
K
D000328:Adult; D016632:Apolipoprotein A-I / Q000235:genetics*; D001483:Base Sequence; D004262:DNA Restriction Enzymes / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D005819:Genetic Markers; D014644:Genetic Variation / Q000235:genetics*; D006801:Humans; D015151:Immunoblotting; D007525:Isoelectric Focusing; D008074:Lipoproteins / Q000097:blood; D008297:Male; D008969:Molecular Sequence Data; D009154:Mutation; D016133:Polymerase Chain Reaction; D012150:Polymorphism, Restriction Fragment Length
D016632:Apolipoprotein A-I; D005819:Genetic Markers; D008074:Lipoproteins; D004262:DNA Restriction Enzymes