Abstract
Homogenates of silkworm pupal fat body were separated into particulate and supernatant fractions by centrifugation. The particulate fraction was further washed with EGTA. Adenylate cyclase activity of the washed particulate fraction was stimulated 2-fold by the addition of supernatant fraction in the presence of low concentrations of Ca2+. The activating factor in supernatant was heat-stable, non-dialyzable and trypsin-sensitive, and shown to be a Ca2+-dependent regulator protein. For the activation of adenylate cyclase by the regulator protein, the optimum concentrations of free Ca2+ were in a range of 2 µm, and higher concentrations of Ca2+ were inhibitory.
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 callDisclaimer: 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.
