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J. Biochem, 1989, Vol. 106, No. 1 151-157
© 1989 Japanese Biochemical Society

research-article

Primary Structure of H2-Proteinase, a Non-Hemorrhagic Metalloproteinase, Isolated from the Venom of the Habu Snake, Trimeresurus flavoviridis1

Hiroyuki Takeya*, Mitsue Arakawa*, Toshiyuki Miyata*, Sadaaki Iwanaga*,2 and Tamotsu Omori-Satoh**

*Department of Biology, Faculty of Science, Kyushu University 33 Higashi-ku, Fukuoka, Fukuoka 812
**Department of Applied Immunology, National Institute of Health Shinagawa-ku, Tokyo 141

2To whom correspondence should be addressed.

The complete amino acid sequence of and the locations of disulfide bridges in H2-proteinase, a major non-hemorrhagic proteinase isolated from the venom of the habu Trimeresurus flavoviridis, have been determined and compared with those of HR2a, one of the hemor-rhagic metalloproteinases in this venom. The strategy involved consisted of structural analysis of peptides in digests with cyanogen bromide, lysyl endopeptidase, trypsin, Staphylococcus aureus V8 protease and thermolysin. Peptides were purified by gel filtration followed by reversed-phase HPLC. H2-proteinase is a non-glycosylated single chain polypeptide consisting of 201 amino acids with an amino-terminal pyroglutamic acid, a calculated molecular weight of 22, 991 and a net charge of +14 at neutral pH. There was no evidence of heterogeneity of the sequence. H2-proteinase has a typical zinc-chelating sequence and its overall sequence identity with HR2a is 73.6%. The 3 disulfide bridges in H2-proteinase link Cys-117 to Cys-196, Cys-158 to Cys-180, and Cys-160 to Cys-163, in the same manner as in the case of HR2a. In striking contrast to HR2a, it contains en extra free cysteine residue at position 94 which becomes reactive to a sulfhydryl reagent in the presence of a denaturant.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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