Abstract
Some properties of calmodulin (CaM)-binding proteins (CaMBPs) of the Ca 2+-independent type were investigated in the synaptosomal membrane (SM) from rat brain using the [ 125I]CaM gel overlay method. When SM was prepared in the presence of Ca 2+, Ca 2+-independent CaM binding was decreased, whereas the Ca 2+-dependent type was not altered. All Ca 2+-independent-type CaMBPs were membrane-bound and scarcely present in the soluble fractions. When SM was heat-denatured, the 24 22.5 -kDa CaMBPs could no longer be detected by [ 125]CaM binding and a new component with higher molecular mass (>200kDa) was shown to bind CaM in a Ca 2+-independent manner. A possible effect of cAMP- and Ca 2+ CaM -dependent phosphorylation on CaM binding was also examined.
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.
