| Literature DB >> 4725041 |
Abstract
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.Entities:
Mesh:
Substances:
Year: 1973 PMID: 4725041 PMCID: PMC1177588 DOI: 10.1042/bj1320301
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857