Modulator protein as a component of the myosin light chain kinase from chicken gizzard.

Abstract:

:The Ca2+-dependent regulation of smooth muscle actomyosin involves a myosin light chain kinase (ATP: myosin light chain phosphotransferase). It has been shown (Dabrowska, R., Aromatorio, D., Sherry, J.M.F., and Hartshorne, D.J. 1977, Biochem. Biophys. Res. Commun. 78, 1263) that the kinase is composed of two proteins of approximate molecular weights 105 000 and 17 000. In this communication it is demonstrated that the 17 000 component is the modulator protein. This conclusion is based on: (1) the identical behavior of the 17 000 kinase component and modulator protein in assays of actomyosin Mg2+-ATPase activity, phosphorylation of myosin, and phosphodiesterase activity, and, (2) the similarity of the 17 000 kinase component and the modulator protein with respect to amino acid composition, absorption spectrum, and electrophoresis in urea-polyacrylamide gels. It is shown also that the modulator protein from smooth muscle and troponin C are distinct proteins.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Dabrowska R,Sherry JM,Aromatorio DK,Hartshorne DJ

doi

10.1021/bi00595a010

subject

Has Abstract

pub_date

1978-01-24 00:00:00

pages

253-8

issue

2

eissn

0006-2960

issn

1520-4995

journal_volume

17

pub_type

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