Abstract
AbstractDemembranated spermatozoa of Ciona do not become motile when provided with MgATP, unless their motility is activated in vivo before demembranation or unless the demembranated spermatozoa are activated in vitro with cAMP or with the catalytic subunit of a cAMP‐dependent protein kinase. CAMP causes a greater than fivefold enhancement of 32P incorporation by demembranated spermatozoa. Analysis by one‐dimensional PAGE and autoradiography shows several axonemal protein bands that become 32P‐labeled during in vitro activation with cAMP and identifies protein bands whose labeling is specifically reduced if motility of the spermatozoa is activated before demembranation, suggesting that these proteins also become phosphorylated during activation of motolity in vivo. These phosphorylated proteins appear to include dynein heavy‐chain components, but axonemal tubulin is not phosphorylated. Partially phosphorylated spermatozoa can be activated by an increase in KCI concentration, which appears to dissociate one phosphorylated component from the axoneme.
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.
