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Characterization of specific binding sites for [3H]-staurosporine on various protein kinases.

Abstract：

:Binding of [3H]-staurosporine to different protein kinases was time-dependent, reversible and saturable. Scatchard analysis of saturation isotherms indicated one class of binding sites for [3H]-staurosporine with dissociation constants (KD) of 9.6, 2.0, 3.0 and 7.4 nM for protein kinase C, cAMP-dependent protein kinase, tyrosine protein kinase and calcium/calmodulin-dependent protein kinase respectively. [3H]-staurosporine binding was fully displaced by unlabelled staurosporine or the related compound K-252a whereas other protein kinase inhibitors (H-7, H-8 and W-7) did not compete with [3H]-staurosporine. These data confirm that sataurosporine shows no selectivity for different protein kinases and suggest the putative existence of distinct, specific binding sites for [3H]-staurosporine on these enzymes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Herbert JM,Seban E,Maffrand JP

doi

10.1016/0006-291x(90)91375-3

subject

Has Abstract

pub_date

1990-08-31 00:00:00

pages

189-95

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)91375-3

journal_volume

171

pub_type

杂志文章

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