Isolation and characterization of human apolipoprotein A-I Fukuoka (110 Glu----Lys). A novel apolipoprotein variant.
Article Details
- CitationCopy to clipboard
Takada Y, Sasaki J, Ogata S, Nakanishi T, Ikehara Y, Arakawa K
Isolation and characterization of human apolipoprotein A-I Fukuoka (110 Glu----Lys). A novel apolipoprotein variant.
Biochim Biophys Acta. 1990 Apr 2;1043(2):169-76.
- PubMed ID
- 2107878 [ View in PubMed]
- Abstract
A novel genetic variant of apolipoprotein(apo) A-I Fukuoka, has been identified in a Japanese family. This variant has a relative charge of +2 compared to normal apolipoprotein A-I (A-I4), on the isoelectric focusing gels and the same molecular mass and immunologic characteristics as normal apolipoprotein A-I. This variant, transmitted as an autosomal co-dominant inheritance was purified by preparative Immobiline isoelectric focusing. Sequence analysis after cleavage with lysyl endopeptidase and CNBr, followed by high-performance liquid chromatography revealed a single substitution of lysine at position 110, instead of the usual glutamic acid. This mutant apolipoprotein A-I has much the same potential as to activate lecithin-cholesterol acyltransferase.