A glycoprotein from the venom of Bothrops barnetti snake , was purified using gel filtration and ionic exchange chromatography . This protein showed 48 kDa as molecular weight by PAGE-SDS under nonreducing conditions being its carbohydrate content 48% of the total mass protein. This enzyme had activity either Benzoil Arginil-p-Nitroanilide (BApNA) and human citrated plasma. In addition this enzyme was strongly inhibited by PMSF and tripsin soybean inhibitor indicating that it is a seninoproeinase

Se ha purificado una glicoproteína del veneno de la serpiente peruana Bothrops barnetti mediante tres pasos cromatográficos que involucran exclusión molecular e intercambio iónico. Mediante PAGE-SDS se determinó que la enzima posee un peso de 48 kDa bajo condiciones no reductoras. El contenido de carbohidratos representa el 48% de la masa total. La enzima presentó actividad sobre el sustrato Benzoil Arginil p Nitroanilida (BApNA) y plasma humano citratado. La enzima fue fuertemente inhibida por el PMSF y el inhibidor de tripsina de soya indicando que se trata de una serinoproteasa.

Has immobilized the snake venom of Bothrops atrox Peruvian to obtaining specific antibodies from the serum of immunized previously albino rabbits by affinity chromatography . Venom ( 100 mg ) was coupled to 1 g of BrCN - Sepharose 4B resin and packed into a chromatography column of 0.8 x 6.0 cm . This column was used for purification of specific antibodies from serum of New Zealand albino male rabbits ( 2 kg ) immunized with B. atrox venom . Serum ( 1 ml ) was applied to the column and protein fractions were eluted sequentially with 0.15 M NaCl , pH 6.0 buffer and 0.1 M glycine -HCl , pH 2.5 . Protein quantitation was performed by spectrophotometric methods . Immobilization of B. atrox venom gel yielded the affinity column to obtain anti- B antibodies . atrox , which were eluted with glycine -HCl buffer 0.1 M , pH 2.5 , recovering 100 mg of this antibody per mL serum. It is concluded tha...

Has immobilized the snake venom of Bothrops atrox Peruvian to obtaining specific antibodies from the serum of immunized previously albino rabbits by affinity chromatography . Venom ( 100 mg ) was coupled to 1 g of BrCN - Sepharose 4B resin and packed into a chromatography column of 0.8 x 6.0 cm . This column was used for purification of specific antibodies from serum of New Zealand albino male rabbits ( 2 kg ) immunized with B. atrox venom . Serum ( 1 ml ) was applied to the column and protein fractions were eluted sequentially with 0.15 M NaCl , pH 6.0 buffer and 0.1 M glycine -HCl , pH 2.5 . Protein quantitation was performed by spectrophotometric methods . Immobilization of B. atrox venom gel yielded the affinity column to obtain anti- B antibodies . atrox , which were eluted with glycine -HCl buffer 0.1 M , pH 2.5 , recovering 100 mg of this antibody per mL serum. It is concluded tha...