Flint A P, Armstrong D T
Biochem J. 1973 Feb;132(2):301-11. doi: 10.1042/bj1320301.
A method involving the use of isolated cholesterol ester-storage granules as substrate is described for the assay of cholesterol esterase in rabbit ovarian tissues. Activities of cholesterol esterase 100-200-fold higher than those previously reported in ovarian tissues were measured by using this method. In addition to that of cholesterol esterase, activities of cholesterol ester synthetase, cholesterol side-chain cleavage enzyme and 3beta-hydroxy steroid dehydrogenase were determined in rabbit ovarian interstitial tissue and corpora lutea. Activities of these enzymes are in general compatible with the flows through them measured under a variety of conditions both in vivo and in vitro. It is concluded that, in the rabbit ovarian tissues investigated, these enzymes are capable of catalysing the conversions usually attributed to them.
描述了一种以分离的胆固醇酯储存颗粒为底物的方法,用于测定兔卵巢组织中的胆固醇酯酶。使用该方法测得的胆固醇酯酶活性比先前报道的卵巢组织中的活性高100 - 200倍。除胆固醇酯酶外,还测定了兔卵巢间质组织和黄体中胆固醇酯合成酶、胆固醇侧链裂解酶和3β-羟基类固醇脱氢酶的活性。这些酶的活性总体上与在体内和体外各种条件下测得的通过它们的通量相符。得出的结论是,在所研究的兔卵巢组织中,这些酶能够催化通常归因于它们的转化反应。