Severson D L, Fletcher T
Atherosclerosis. 1978 Sep;31(1):21-32. doi: 10.1016/0021-9150(78)90033-3.
Cholesterol ester hydrolase activity was determined in preparations of rabbit and guinea pig aorta utilizing micellar and glycerol-dispersed cholesterol oleate substrates. Both substrate preparations demonstrated an acid pH optimum of 4--5 for the soluble and particulate rabbit media cholesterol ester hydrolase, suggesting a lysosomal origin for this activity. Approximately one-fifth of the total recovered activity was particulate. Particulate media preparations from guinea pig aorta also demonstrated cholesterol ester hydrolase activity at acid pH values with a definite optimum at pH 5 for the glycerol-dispersed substrate. However, in contrast to the rabbit media enzyme, activity was also observed at neutral pH with another optimum at pH 7. The supernatant enzyme from guinea pig media exhibited only a single pH optimum of 7. Cholesterol ester hydrolase activity from either rabbit or guinea pig media was not influenced by preincubation with cyclic AMP, ATP and protein kinase. The addition of chloroquine resulted in the inhibition of both the rabbit and guinea pig enzyme. Cholesterol ester hydrolase activity from rabbit and guinea pig media was also inhibited by phenyl methane sulfonyl fluoride; activity measured at pH 7 (guinea pig) was more sensitive to inhibition than activity measured at pH 5 (guinea pig and rabbit).
利用胶束和甘油分散的胆固醇油酸酯底物，在兔和豚鼠主动脉制剂中测定胆固醇酯水解酶活性。两种底物制剂对可溶性和颗粒性兔培养基胆固醇酯水解酶均显示出4 - 5的最适酸性pH值，表明该活性起源于溶酶体。回收的总活性中约五分之一是颗粒性的。豚鼠主动脉的颗粒性培养基制剂在酸性pH值下也显示出胆固醇酯水解酶活性，对于甘油分散的底物，在pH 5时有明确的最适值。然而，与兔培养基酶不同的是，在中性pH值下也观察到活性，在pH 7时有另一个最适值。豚鼠培养基的上清液酶仅显示出单一的pH最适值7。兔或豚鼠培养基的胆固醇酯水解酶活性不受与环磷酸腺苷、三磷酸腺苷和蛋白激酶预孵育的影响。添加氯喹导致兔和豚鼠酶均受到抑制。兔和豚鼠培养基的胆固醇酯水解酶活性也受到苯甲基磺酰氟的抑制；在pH 7（豚鼠）下测得的活性比在pH 5（豚鼠和兔）下测得的活性对抑制更敏感。
