The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Interaction of Rat Lecithin-Cholesterol Acyltransferase with Rat Apolipoprotein A-I and with Lecithin-Cholesterol Vesicles
Yuji FurukawaTakashi UranoYoshifumi HidaHarumi ItchChizuko TakahashiShuichi Kimura
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1992 Volume 111 Issue 3 Pages 413-418

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Abstract

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 vesiclesrThe 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 enzymevesicle 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.

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© The Japanese Biochemical Society
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