Low density lipoprotein-activated lysolecithin acylation by human plasma lecithin-cholesterol acyltransferase. Identity of lysolecithin acyltransferase and lecithin-cholesterol acyltransferase
Subbaiah, P.V.; Albers, J.J.; Chen, C.H.; Bagdade, J.D.
Journal of Biological Chemistry 255(19): 9275-9280
1980
ISSN/ISBN: 0021-9258 PMID: 7410425 Accession: 043559193
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There is in normal plasma an enzyme activity which converts labeled lysolecithin to lecithin by an energy-independent low density lipoprotein-activated pathway. Studies were undertaken to compare the identity of this enzyme with lecithin-cholesterol acyltransferase. During purification of the enzyme by ultracentrifugation and by chromatography on high density lipoprotein affinity column, DEAE-Sepharose column, and hydroxylapatite column, both the lysolecithin acyltransferase activity and the lecithin-cholesterol acyl transferase activity were found in the same fractions and were enriched to the same extent at each step. The final purified preparation which had 16,000- to 24,000-fold higher specific activities than starting plasma gave a single protein band on polyacrylamide gel electrophoresis and this single band contained both the activities. Also, the effects of pH, heat, and chemical inhibitors on the enzyme activities were similar. Plasma from patients with familial lecithin-cholesterol acyltransferase deficiency also lacked lysolecithin acyltransferase activity. These results indicate that a single enzyme carries out both lecithin-cholesterol acyltransferase and lysolecithin acyltransferase activities. The purified enzyme required apolipoprotein A-I for lecithin-cholesterol acyltransferase activity, but required low density lipoprotein for lysolecithin acyltransferase activity.