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Identification and partial purification of a chromatin bound calmodulin activated histone 3 kinase from calf thymus.

Abstract：

:A calcium-calmodulin (Ca2(+)-CaM) stimulated histone H3 phosphorylating activity was identified as a component of a nuclear protein complex purified from a 150 mM NaCl extract of calf thymus chromatin. This activity bound to a CaM-Sepharose affinity column in a Ca2+ dependent manner and was eluted off the column in the presence of EGTA. Equilibrium centrifugation of the EGTA eluate on a sucrose density gradient revealed that the activity is a component of a larger complex identified at 25% sucrose. This complex consisted of two major proteins, having Mr of 65 and 75 kDa. Using [125I] CaM and the gel overlay technique it was shown that the 75 kDa protein is the major CaM binding protein in the complex.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wakim BT,Picken MM,DeLange RJ

doi

10.1016/0006-291x(90)91359-z

subject

Has Abstract

pub_date

1990-08-31 00:00:00

pages

84-90

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)91359-Z

journal_volume

171

pub_type

杂志文章

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