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 Ca2+, 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 (greater than 200 kDa) was shown to bind CaM in a Ca(2+)-independent manner. A possible effect of cAMP- and Ca2+/CaM-dependent phosphorylation on CaM binding was also examined.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Natsukari N,Miwa A,Fujita Mdoi
10.1016/0006-291x(92)90543-tsubject
Has Abstractpub_date
1992-03-16 00:00:00pages
725-32issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(92)90543-Tjournal_volume
183pub_type
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