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J. Biochem, 1992, Vol. 112, No. 6 729-732
© 1992 Japanese Biochemical Society

other

Purification and Characterization of a Possible Protooncogene fjln Product, p59fyn, from a Rat Brain Particulate Fraction1

Takahiro Miyauchi*, Masahiro Ariki*, Hirofumi Usui*, Kentaro Semba**, Yumiko Matsuzawa**, Tadashi Yamamoto**, Kumao Toyoshima**,2 and Masao Takeda*,3

*Department of Biochemistry, Hiroshima University School of Medicine 1-2-3 Kasumi, Minami-ku, Hiroshima, Hiroshima 734
**Institute of Medical Sciences, The University of Tokyo 4-6- 1 Shiroganedai, Minato-ku, Tokyo 108

3To whom correqmndence should be addresssd

Four tyrosine-protein kinases that reacted with antibodies specific to p62c-yes, p60c-src, p60c-src, and p59fyn, respectively, were solubilized from a rat brain particulate fraction and separated by casein-Toyopearl column chromatography. Possible p59fyn, with a pI of 6.5, was purified 490-fold as a single 69-kDa protein band on SDS-PAGE. The purified enzyme contained almost no phosphotyrosine residues but was autophosphorylated with Mg2+-·ATP exclusively at tyrosine residues, with a concomitant increase in the kinase activity toward tyrosine-glutamate (1 : 4) copolymers. The rate of the copolymer phosphorylation was proportional to the square of the enzyme concentration, suggesting activation through intermolecular catalysis. In the presence of Mn2+, however, the reaction showed a firstorder dependence on the enzyme concentration.

1This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan (1987–1991).

2Present address: Department of Oncogene Research, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 566.


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