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Purification of a novel isoform of the regulatory subunit of cAMP-dependent protein kinase from the bivalve mollusk Mytilus galloprovincialis.

Abstract：

:Cytosolic extracts from the posterior adductor muscle of the bivalve mollusk Mytilus galloprovincialis contain significant amounts of both cGMP-binding and cGMP-stimulated protein kinase activities. However, photoaffinity labeling with 8-azido-[32P]cGMP revealed only a major cGMP-binding protein with an apparent molecular mass of 54 kDa (p54), lacking protein kinase activity itself. Instead, the purified and cGMP-free p54 protein has the ability to inhibit a mussel protein kinase homologous to the mammalian cAMP-dependent protein kinase (cAPK) catalytic subunit, the inhibition being relieved by cAMP or cGMP, which suggests that it can act as a regulatory subunit of cAPK. However, p54 failed to be recognized by a specific antibody against the regulatory subunit (type RII) previously isolated from mussel. Therefore, p54 must be a novel isoform of cAPK regulatory subunit that seems to have high affinity for both cGMP and cAMP.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Rodríguez JL,Barcia R,Ramos-Martínez JI,Villamarín JA

doi

10.1006/abbi.1998.0879

subject

Has Abstract

pub_date

1998-11-01 00:00:00

pages

57-62

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003986198908797

journal_volume

359

pub_type

杂志文章

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