Abstract
Direct activation of adrenal Sterol Ester Hydrolase (EC 1.1.1.13) by dibutyryl cAMP, ATP and Mg +2 has been demonstrated in adrenal homogenates from three species. Variability in the degree of activation was minimized by preincubation of the tissue homogenate for two hours prior to addition of the cofactors and subsequent enzyme assay. Although baseline sterol ester hydrolytic activity, independent of cofactors, was present in all subcellular fractions, the cAMP-dependent enzyme was primarily associated with the 105,000 × g soluble fraction of the cell. A requirement for protein kinase in the system was demonstrated with a partially-purified enzyme from bovine adrenal.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
