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Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase.

Abstract：

:Phosphorylation of HMG 14 proteins from calf thymus and avian erythrocytes was studied using a cyclic GMP-dependent protein kinase from bovine lung. HMG 14 from calf thymus was a good substrate for the enzyme, but HMG 14 from avian erythrocytes was not phosphorylated. Of the potential phosphorylation sites, the one in the amino terminal sequence Pro-Lys-Arg-Lys-Val-Ser-Ser-Ala-Glu (residues 1-9) is present in HMG 14 from calf thymus but not in HMG 14 from avian erythrocytes suggesting that the phosphorylated amino acid residue in HMG 14 from calf thymus is Ser-6 (and possibly Ser-7).

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Palvimo J,Linnala-Kankkunen A,Mäenpää PH

doi

10.1016/0006-291x(83)91159-2

subject

Has Abstract

pub_date

1983-01-27 00:00:00

pages

378-82

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)91159-2

journal_volume

110

pub_type

杂志文章

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