Abstract:
:In brain tissue a spectrin-like calmodulin-binding protein calspectin, or fodrin, is concentrated in a synaptosome fraction, where most of the calspectin is associated with the synaptic membranes. This endogenous calspectin was phosphorylated by protein kinase system(s) associated with the membranes. Here, we report the solubilization and partial purification of the membrane-associated calspectin kinase activity. The activity was resolved on a gel filtration column into two fractions, peaks I and II having estimated Mr of 800 000 and 88 000. The activity of peak I was dependent on the presence of both Ca2+ and calmodulin. Peak II revealed a basal activity in the absence of Ca2+ and calmodulin, which was stimulated 2-fold by addition of Ca2+. Calmodulin had no effect on the peak II activity.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sobue K,Kanda K,Kakiuchi Sdoi
10.1016/0014-5793(82)81331-8subject
Has Abstractpub_date
1982-12-13 00:00:00pages
185-90issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(82)81331-8journal_volume
150pub_type
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