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Journal of Biochemistry Advance Access originally published online on March 11, 2009
Journal of Biochemistry 2009 146(1):43-49; doi:10.1093/jb/mvp045
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Re-Evaluation of M-LAO, L-Amino Acid Oxidase, from the Venom of Gloydius blomhoffi as an Anticoagulant Protein

Daisuke Fujisawa, Yasuo Yamazaki and Takashi Morita*

Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1 Kiyose, Tokyo 204-8588, Japan

*To whom correspondence should be addressed. E-mail: tmorita{at}my-pharm.ac.jp

Received February 9, 2009; Accepted February 26, 2009


  Abstract

Many anticoagulant proteins have been found from snake venoms. Recently, L-amino acid oxidase (LAO) from the venom of Gloydius blomhoffi, M-LAO, was reported to inhibit coagulation factor IX; however, the mechanism of its anticoagulant activity is still unclear. Here, we re-evaluated the anticoagulant activity of M-LAO. We first purified M-LAO from the venom of G. blomhoffi, and examined the effect of LAO inhibitors and the hydrogen peroxide scavenger, catalase, on the anticoagulant activity of M-LAO. We found that the isolated M-LAO fraction prolongs the APTT, PT and fibrinogen clotting time and cleaves the A{alpha}-chain of fibrinogen. LAO inhibitors or catalase did not inhibit these effects. Detailed analysis revealed that the M-LAO fraction contained a small amount of 39-kDa metalloproteinase. The prolongation of clotting time and degradation of fibrinogen were inhibited by a metalloproteinase inhibitor. Therefore, we concluded that the anticoagulant activity of the M-LAO fraction was caused by the 39-kDa metalloproteinase.

Key Words: anticoagulant, L-amino acid oxidase, blood coagulation, factor IX, snake venom

Abbreviations: APTT, activated partial thromboplastin time; LAO, L-amino acid oxidase; IX/X-bp, blood coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis; PT, prothrombin time


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