Habutobin Splits the Arg16-Gly17 Bond in the Aa Chain of Rabbit Fibrinogen

Kiyohiko Kinjoh; Tadayoshi Kosugi; Mariko Nakamura; Kazuhiko Hanashiro; Masanori Sunagawa; Yoshihiro Tokeshi; Yukinori Eguchi

doi:10.1055/s-0038-1656124

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1997; 77(06): 1127-1128
DOI: 10.1055/s-0038-1656124

Coagulation

Schattauer GmbH Stuttgart

Habutobin Splits the Arg¹⁶-Gly¹⁷ Bond in the Aa Chain of Rabbit Fibrinogen

Authors

Kiyohiko Kinjoh

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
Tadayoshi Kosugi

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan

²The Research Center of Comprehensive Medicine, University of the Ryukyus, Okinawa, Japan
Mariko Nakamura

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
Kazuhiko Hanashiro

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
Masanori Sunagawa

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
Yoshihiro Tokeshi

¹The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
Yukinori Eguchi

³The Research Laboratory Center, School of Medicine, University of the Ryukyus, Okinawa, Japan

Abstract

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Summary

We reported previously that habutobin, a thrombin-like enzyme from Trimeresurus flavoviridis venom, clotted only rabbit fibrinogen, whereas human, monkey, bovine, dog, rat and guinea-pig fibrinogens were unaffected. In the present study, we investigated the cleavage site of the rabbit Aα chain by habutobin. The fibrinopeptide released by habutobin was identical to the fibrinopeptide A released by thrombin, and its amino acid sequence corresponded to Aα 1-16 of rabbit fibrinogen. It was clarified therefore that habutobin cleaves the Arg¹⁶-Gly¹⁷ bond in the Aa chain of rabbit fibrinogen.

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References

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