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Evidence that relaxation of hog biliary muscle is mediated by the interaction between the protein inhibitor of cyclic AMP dependent protein kinase and cholecystokinin C-terminal peptides.

Abstract：

:The interaction of various cholecystokinin (CCK) peptides with the protein inhibitor (PK-I) of cyclic AMP dependent protein kinase (A-PK) has been studied. The order of the affinities (ED50) for relaxation of hog biliary muscle by a series of C-terminal peptides of CCK correlated with the order of the potencies for A-PK-catalyzed phosphorylation of the sarcoplasmic reticulum enriched fraction (SR-F) in the muscle. CCK-4 peptide inhibited the PK-I of A-PK. The apparent Km value of the peptide was 11.5 microM. Scatchard plot analysis for the binding of [14C]CCK-6 peptide to the PK-I showed a dissociation constant (Kd) of 11.2 microM. These results indicated that the Kd value agreed with the ED50 value of CCK-6 and the Km value of CCK-4. It is proposed that a receptor for CCK C-terminal peptides is probably a component in the PK-I; binding of the peptides to this site usually results in the relaxation by these allosteric inhibitors of the PK-I.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Kimura M,Kobayashi S,Kimura I

doi

10.1016/0006-2952(83)90578-6

subject

Has Abstract

pub_date

1983-03-01 00:00:00

pages

795-8

issue

5

eissn

0006-2952

issn

1873-2968

pii

0006-2952(83)90578-6

journal_volume

32

pub_type

杂志文章

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