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This enzyme was isolated through a combination of three chromatographic steps (ion-exchange, molecular exclusion, and affinity chromatography). Analyses by reverse phase chromatography, followed by mass spectrometry, showed the presence of enzyme isoforms with average molecular mass of 22.8\u2009kDa. The SDS-PAGE analyses showed a single chain of 27.6\u2009kDa, in the presence and absence of reducing agent. The protein has a blocked N-terminal. One of the peptides obtained by enzymatic digestion of a reduced and S-alkylated isoform was completely sequenced by mass spectrometry (MS\/MS). Bmoo FIBMP-I showed similarity with hemorrhagic factor and several metalloproteinases (MP). This enzyme degraded A<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M1\"><mml:mrow><mml:mi>\u03b1<\/mml:mi><\/mml:mrow><\/mml:math>-chain faster than the B<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M2\"><mml:mrow><mml:mi>\u03b2<\/mml:mi><\/mml:mrow><\/mml:math>-chain and did not affect the<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M3\"><mml:mrow><mml:mi>\u03b3<\/mml:mi><\/mml:mrow><\/mml:math>-chain of bovine fibrinogen. The absence of proteolytic activity after treatment with EDTA, together with the observed molecular mass, led us to suggest that Bmoo FIBMP-I is a member of the P-I class of the snake venom MP family. Bmoo FIBMP-I showed pH-dependent proteolytic activity on azocasein, but was devoid of coagulant, defibrinating, or hemorrhagic activities. The kinetic parameters of proteolytic activity in azocasein were determined (<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M4\"><mml:msub><mml:mi>V<\/mml:mi><mml:mrow><mml:mtext>max<\/mml:mtext><\/mml:mrow><\/mml:msub><mml:mo>=<\/mml:mo><mml:mn>0.4596<\/mml:mn><mml:msup><mml:mtext>\u2009Uh<\/mml:mtext><mml:mrow><mml:mo>\u2212<\/mml:mo><mml:mn>1<\/mml:mn><\/mml:mrow><\/mml:msup><mml:msup><mml:mtext>nmol<\/mml:mtext><mml:mrow><mml:mo>\u2212<\/mml:mo><mml:mn>1<\/mml:mn><\/mml:mrow><\/mml:msup><mml:mo>\u00b1<\/mml:mo><mml:mn>0.1031<\/mml:mn><\/mml:math>and<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M5\"><mml:mrow><mml:msub><mml:mi>K<\/mml:mi><mml:mi>m<\/mml:mi><\/mml:msub><mml:mo>=<\/mml:mo><mml:mn>14.59<\/mml:mn><mml:mtext>\u2009mg\/mL<\/mml:mtext><mml:mo>\u00b1<\/mml:mo><mml:mtext>4<\/mml:mtext><mml:mtext>.610<\/mml:mtext><\/mml:mrow><\/mml:math>).<\/jats:p>","DOI":"10.5402\/2012\/673941","type":"journal-article","created":{"date-parts":[[2012,11,4]],"date-time":"2012-11-04T21:01:08Z","timestamp":1352062868000},"page":"1-10","source":"Crossref","is-referenced-by-count":6,"title":["Bmoo FIBMP-I: A New Fibrinogenolytic Metalloproteinase from<i>Bothrops moojeni<\/i>Snake Venom"],"prefix":"10.5402","volume":"2012","author":[{"given":"F. 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R.","family":"Gomes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biologia Molecular de Produtos Naturais, Departamento de Bioqu\u00edmica e Imunologia, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, MG, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C. E.","family":"Salas","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biologia Molecular de Produtos Naturais, Departamento de Bioqu\u00edmica e Imunologia, Instituto de Ci\u00eancias Biol\u00f3gicas, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, MG, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. M. 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