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J. Biochem, 1986, Vol. 99, No. 5 1359-1369
© 1986 Japanese Biochemical Society

research-article

Ca2+-Independent Gizzard Myosin Light Chain Kinase Produced by Cross-Linking of the Enzyme with Calmodulin Using Glutaraldehyde1

Seiji NAKAMURA and Yoshiaki NONOMURA

Department of Pharmacology, Faculty of Medicine, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113

Cross-linked complex of gizzard myosin light chain kinase (MLCK) and calmodulin (CM) was produced by glutaraldehyde treatment of a mixture of these proteins in a high Ca2+ (0.1 mM) solution. Although the specific activity was reduced, this complex showed MLCK activity in a Ca2+-independent manner, different from the original MLCK whose activity was Ca2+-independent Chiorpromazine, one of the CM antagonists, was no longer able to inhibit the MLCK activity of this complex. These observations support the previously proposed hypothesis on the regulatory mechanism of MLCK activity via Ca2+ This complex could be regarded as another kind of Ca2+-independent MLCK different from that obtained by chymotryptic digestion of MLCK (Walsh, M.P., Dabrowska, R., Hinkins, S., & Hartshorne, D.J. (1982) Biochemistry 21, 1919–1925).

This complex caused superprecipitation of gizzard actomyosin and enhanced actin-activated ATPase of myosin Ca2+independently.

1This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan and grants from the Ministry of Health and Welfare of Japan, and the Iatrochemical Foundation.


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