Calcium ion dependent covalent modification of calmodulin with norchlorpromazine isothiocyanate.

Abstract:

:Calmodulin forms a covalent, one to one, complex with 3H-labeled norchlorpromazine isothiocyanate. Complex formation was monitored by high-performance liquid chromatography using a CN reverse-phase column which resolves calmodulin, the calmodulin-norchlorpromazine adduct, and norchlorpromazine isothiocyanate. Formation of the adduct requires Ca2+ and is not observed with norchlorpromazine. The one to one calmodulin-norchlorpromazine complex does not activate phosphodiesterase but can interact with the enzyme and competitively inhibit its stimulation by calmodulin. High concentrations of trifluoperazine inhibit whereas low concentrations stimulate complex formation. This apparent potentiation of the interaction of calmodulin with norchlorpromazine by another phenothiazine suggests that calmodulin contains at least two phenothiazine binding sites and that the binding of phenothiazine to calmodulin is cooperative.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Newton DL,Burke TR Jr,Rice KC,Klee CB

doi

10.1021/bi00293a003

subject

Has Abstract

pub_date

1983-11-22 00:00:00

pages

5472-6

issue

24

eissn

0006-2960

issn

1520-4995

journal_volume

22

pub_type

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