BjussuSP-I: A new thrombin-like enzyme isolated from Bothrops jararacussu snake venom

A thrombin-like enzyme named BjussuSP-I, isolated from B. jararacussu snake venom, is an acidic single chain glycoprotein with approximately 6% sugar, Mr=61,000 under reducing conditions and pI∼3.8, representing 1.09% of the chromatographic A280 recovery. BjussuSP-I is a glycosylated serine protease...

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Bibliographic Details
Published in:	Comparative biochemistry and physiology. Part A, Molecular & integrative physiology Vol. 151; no. 3; pp. 443 - 454
Main Authors:	Sant' Ana, Carolina D., Ticli, Fabio K., Oliveira, Leandro L., Giglio, Jose R., Rechia, Carem G.V., Fuly, André L., Selistre de Araújo, Heloisa S., Franco, João J., Stabeli, Rodrigo G., Soares, Andreimar M., Sampaio, Suely V.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 01-11-2008
Subjects:	Amino Acid Sequence Animals Antibodies Blood Coagulation Bothrops - metabolism Bothrops jararacussu Chromatography Coagulation Crotalid Venoms - chemistry Crotalid Venoms - enzymology Crotalid Venoms - isolation & purification Enzymatic characterization Humans Male Mice Molecular Sequence Data Polyclonal antibody Proteolysis Rabbits Serine Endopeptidases - immunology Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Snake venoms Thrombin - chemistry Thrombin-like enzyme LAAO Bothrops jararacussu TAME BAPNA Enzymatic characterization Polyclonal antibody Coagulation TFA MCD BjussuSP-I SVTLE TCA PMSF Proteolysis Thrombin-like enzyme Snake venoms
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Summary:	A thrombin-like enzyme named BjussuSP-I, isolated from B. jararacussu snake venom, is an acidic single chain glycoprotein with approximately 6% sugar, Mr=61,000 under reducing conditions and pI∼3.8, representing 1.09% of the chromatographic A280 recovery. BjussuSP-I is a glycosylated serine protease containing both N-linked carbohydrates and sialic acid in its structure. BjussuSP-I showed a high clotting activity upon human plasma, which was inhibited by PMSF, leupeptin, heparin and 1,10-phenantroline. This enzyme showed high stability regarding coagulant activity when analyzed at different temperatures (−70 to 37 °C), pHs (4.5 to 8.0), and presence of two divalent metal ions (Ca2+ and Mg2+). It also displayed TAME esterase and proteolytic activities toward natural (fibrinogen and fibrin) and synthetic (BAPNA) substrates, respectively, being also inhibited by PMSF and leupeptin. BjussuSP-I can induce production of polyclonal antibodies able to inhibit its clotting activity, but unable to inhibit its proteolytic activity on fibrinogen. The enzyme also showed crossed immunoreactivity against 11 venom samples of Bothrops, 1 of Crotalus, and 1 of Calloselasma snakes, in addition of LAAO isolated from B. moojeni venom. It displayed neither hemorrhagic, myotoxic, edema-inducing profiles nor proteolytic activity on casein. BjussuSP-I showed an N-terminal sequence (VLGGDECDINEHPFLA FLYS) similar to other thrombin-like enzymes from snake venoms. Based on its biochemical, enzymatic and pharmacological characteristics, BjussuSP-I was identified as a new thrombin-like enzyme isoform from Bothrops jararacussu snake venom.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1095-6433 1531-4332
DOI:	10.1016/j.cbpa.2007.02.036