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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

Kiyohiko Kinjoh
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
,
Tadayoshi Kosugi
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
2   The Research Center of Comprehensive Medicine, University of the Ryukyus, Okinawa, Japan
,
Mariko Nakamura
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
,
Kazuhiko Hanashiro
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
,
Masanori Sunagawa
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
,
Yoshihiro Tokeshi
1   The 1st Department of Physiology, University of the Ryukyus, Okinawa, Japan
,
Yukinori Eguchi
3   The Research Laboratory Center, School of Medicine, University of the Ryukyus, Okinawa, Japan
› Author Affiliations
Further Information

Publication History

Received 31 December 1996

Accepted after revision 26 February 1997

Publication Date:
12 July 2018 (online)

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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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