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J. Biochem, 1988, Vol. 104, No. 3 427-432
© 1988 Japanese Biochemical Society

research-article

Photocross-Linking from Dinitrophenylated SH1 in Myosin Head. II. Cross-Linked Site on 50-kDa Fragment1

Daisaku Muno and Takamitsu Sekine2

Department of Biochemistry, School of Medicine, Juntendo University Bunkyo-ku, Tokyo 113

We reported in the preceding paper [Muno, D., et al. (1987) J. Biochem. 101, 661–669] that the dinitrophenyl group exclusively introduced to SH1 on the 20-kDa fragment of myosin subfragment 1 was cross-linked to the 50-kDa fragment by irradiation, and that limited trypsinolysis of the cross-linked S1 generated an 83-kDa peptide, a cross-linking product between the 20- and 50-kDa fragments. This paper will deal with the location of the cross-linked residue on the 50-kDa fragment. When the 83-kDa fragment labeled at SH with a fluorogenic SH reagent was subjected to bromocyanolysis, a main fluorescent band, which implied a cross-linked peptide, appeared in the position with an apparent molecular mass of 18.5-kDa on SDS-PAGE. On the other hand, another cross-linked peptide was obtained from a complete tryptic digest of a 83-kDa fragment rich fraction. Amino acid sequence analysis of the two cross-linked peptides revealed that the DNP moiety attached at SH1 was cross-linked with a residue in the segment of the heavy chain spanning the 485–493 region from the N-terminus of the heavy chain.

1This study was supported in part by Grants-in-Aid for Scientific Research (Nos. 457083 and 567108) from the Ministry of Education, Science and Culture of Japan.

2Present address: Department of Biochemistry, Saitama Medical School, Morohongo, Iruma-gun, Saitama 350-04.


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