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J. Biochem, 1992, Vol. 112, No. 6 796-799
© 1992 Japanese Biochemical Society

research-article

Site of Attachment of Mercuribenzoate in Crystals of an Actin:DNase I Complex

Hiroehi Hayashi* and Hiroehi Kondo**

*Sugashima Marine Biological Laboratoty, School of Science, Nagoya University Toba Mie 517
**Department of Molecular Biology, School of Science, Nagoya University Chikusa-ku, Nagqya 464-01

Crystals of a complex of chicken gizzard G-actin and DNase I were soaked in a solution of radioactive 4-hydroxymercuribenzoate (MB). The soaked crystals, which contained 0.93 mol of MB per mol of G-actin, were dissolved in "G-baffer" and digested with trypsin, and the resulting peptides were fractionated by thin-layer chromatography. The MB is exchangeable between peptides that contain cysteine residues, but the data obtained here suggested that MB attached to the cysteine residue at the 373rd position of the G-actin molecule.


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