Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles.
The interaction of rat plasma lecithin-cholesterol acyltransferase with lecithin-cholesterol vesicles and with rat apo-A-I was studied in comparison with that of human plasma lecithin-cholesterol acyltransferase to clarify the reaction mechanism of rat plasma lecithin-cholesterol acyltransferase. The interaction of both human and rat lecithin-cholesterol acyltransferase with lecithin-cholesterol vesicles was investigated by gel permeation chromatography on Superose 12. Both enzymes had almost the same affinity to the vesicles. The affinity of rat enzyme to rat apo-A-I was stronger than that of human enzyme to human apo-A-I when estimated on the apo-A-I-Sepharose 4B column. When human apo-A-I was added to the human enzyme/vesicle mixture which contained the enzyme-vesicle complex, the enzyme was effectively dissociated from the complex. But when rat apo-A-I was added to the rat enzyme/vesicle mixture, apo-A-I-enzyme-vesicle complex was still recognized by its elution pattern on gel permeation chromatography. This suggests that the mixture of rat enzyme, rat apo-A-I, and vesicles, which are the major components in the rat lecithin-cholesterol acyltransferase reaction, forms a stronger complex than do the components of the human reaction.
Furukawa
Y
Y
Department of Food Chemistry, Faculty of Agriculture, Tohoku University, Miyagi.
Urano
T
T
Hida
Y
Y
Itoh
H
H
Takahashi
C
C
Kimura
S
S
D000818:Animals; D016632:Apolipoprotein A-I / Q000032:analysis / Q000494:pharmacology*; D002850:Chromatography, Gel; D006801:Humans; D007862:Phosphatidylcholine-Sterol O-Acyltransferase / Q000097:blood*; D051381:Rats
D016632:Apolipoprotein A-I; D007862:Phosphatidylcholine-Sterol O-Acyltransferase