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J. Biochem, 1988, Vol. 104, No. 5 858-861
© 1988 Japanese Biochemical Society

research-article

Isolation from Bovine Brain of 155 kDa Component Exhibiting Myosin Light Chain Kinase Activity1

Hideto Kuwayama2 and Setsuro Ebashi3

National Institute for Physiological Sciences, Okazaki Aichi 444

3 To whom correspondence should be addressed

1) Taking myosin light chain kinase (MLCK) activity as the index, bovine brain extract was fractionated by the use of anion-exchange chromatography, cation-exchange chromatogra phy, and calmodulin affinity chromatography. The kinase activity of the fraction thus obtained was elevated up to about 12,400 times over that of the original crude extract. 2) The fraction mentioned above was subjected again to anion exchange chromatography. The kinase activities were divided into two parts, i.e., part I which contained the 155 kDa component and part II which was virtually free of 155 kDa component. The MLCK activity of part I was considerably lower than that of part II. 3) Part I was subjected to gel filtration using AcA 34 gel and the 155 kDa component was isolated. The fraction contained the 155 kDa component in a homogeneous state and showed myosin specific kinase activity, which was about 2×105 times that of the original crude extract. 4) The high kinase activity of part II seemed to be ascribable to the 130 kDa component, in accord with the report of Hathaway, Adelstein, and Klee (J. Biol. Chem. 256, 8183–8189, 1981).

1 Supported by a Grant-in-aid from the Ministry of Education, Science and Culture of Japan. A large part of the results presented in this article was reported at the 57th Annual Meeting of the Japanese Biochemical Society, October 1984

2 Present address: Laboratory of Chemistry, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080


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