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The calmodulin-stimulated ATPase of maize coleoptiles forms a phosphorylated intermediate.

Abstract：

:The calmodulin-stimulated ATPase of maize coleoptiles is a 140,000 Mr polypeptide. In the present study, formation of a phosphorylated intermediate by the enzyme is demonstrated. Phosphorylation is sensitive to chasing with unlabelled ATP and to hydroxylamine; lanthanum enhances its intensity while calmodulin enhances phosphorylation in the presence of lanthanum but not in its absence. Ethyleneglycol-bis-(beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) inhibits phosphorylation of the purified enzyme, but microsome preparations give a band of phosphorylation of 153,000 Mr in its presence. This latter phosphorylated band was not abolished after a variety of permeabilising treatments in the presence of Triton X-100; phosphorylation of the enzyme was absent when sodium deoxycholate was used as the solubilising detergent. The identity of the 153,000 Mr band is discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Briars SA,Evans DE

doi

10.1016/0006-291x(89)92421-2

subject

Has Abstract

pub_date

1989-02-28 00:00:00

pages

185-91

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)92421-2

journal_volume

159

pub_type

杂志文章

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