PMID: 39582Jul 1, 1979

Studies of cholesterol esterase in rat arterial wall

M ShinomiyaA Kumagai


Cholesterol esterase activity was estimated in homogenates of rat arterial wall using radioactive cholesteryl oleate incorporated into phospholipid vesicles as a substrate. The labeled oleic acid was separated from the ester by addition of benzene-chloroform-methanol mixture. Under these conditions, two pH optima were found at about 4.5 and 7.5. Most of the activities at pH 4.5 and 7.5 were found in the lysosomal and microsomal fraction, respectively. No enzyme activity was detected when the substrate vesicles were prepared with phosphatidylethanolamine or sphingomyelin, but the activity was higher when the substrate vesicles were prepared with phosphatidylserine and highest when they were prepared with phosphatidylcholine. The relationship between enzyme regulation and lipid deposition in the arterial wall is discussed.


Jul 22, 1988·Biochimica Et Biophysica Acta·Y IshikawaS Yoshida
Jan 1, 1987·Pharmacology & Therapeutics·R J MorinS K Peng
May 1, 1982·Atherosclerosis·N MorisakiA Kumagai
May 1, 1980·Atherosclerosis·M ShinomiyaA Kumagai
Feb 1, 1981·Atherosclerosis·M ShinomiyaA Kumagai
Jan 1, 1994·Journal of Atherosclerosis and Thrombosis·K UchidaN Takeuchi


Feb 14, 1973·Biochimica Et Biophysica Acta·H V KothariD Kritchevsky
Apr 18, 1972·Biochimica Et Biophysica Acta·J W Proudlock, A J Day
May 1, 1968·Journal of Atherosclerosis Research·S Dayton, S Hashimoto
Oct 1, 1955·Proceedings of the Society for Experimental Biology and Medicine·F WROBLEWSKI, J S LADUE
Nov 1, 1954·Journal of Clinical Pathology·P R KIND, E J KING

Related Concepts

cholesteryl oleate
Enzyme Activity
Substrate Specificity
Blood Enzyme Activity (Lab Test)

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