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J. Biochem, 1990, Vol. 108, No. 1 139-143
© 1990 Japanese Biochemical Society

research-article

Amino Acid Sequence of a Lectin from Japanese Frog (Rana japonica) Eggs1

Yuji Kamiya*, Fumitaka Oyama*, Rieko Oyama*, Fusao Sakakibara**, Kazuo Nitta**, Hiroaki Kawauchi**, Yoshio Takayanagi** and Koiti Titani*,2

*Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health Uniuersity Toyoake, Aichi 470-11;
**Cancer Research Institute, Tohoku College of Pharmaceutical Science Sendai, Miyagi 981

22 To whom correspondence should be addressed

The complete amino acid sequence and the location of disulfide bonds of a lectin from Japanese frog (Rana japonica) eggs, which specifically agglutinates transformed cells, are presented. The sequence was determined by analysis of peptides generated by digestion of the S-carboxyamidomethylated protein with Achromobacter protease I, or chymotrypsin, and by chemical cleavage with BNPS-skatole or cyanogen bromide. The lectin is a single-chain protein consisting of 111 residues, with a pyroglutamyl residue at the amino terminus. Four disulfide bonds link half-cystinyl residue 19 to 72, 34 to 82, 52 to 97, and 94 to 111. The sequence and the location of the disulfide bonds are highly homologous to those of bull frog (Rana catesbeiana) egg S-lectin. They are also homologous to human an-giogenin, a tumor angiogenesis factor, and a family of pancreatic ribonucleases.

1This work was supported by a Grant-in-Aid from Fujita Health University and a Science Research Promotion Fund from the Japan Private School Promotion Foundation.


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