TY - JOUR
T1 - Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
AU - Gutiérrez, JoséMaría
AU - Romero, Marjorie
AU - Díaz, Cecilia
AU - Borkow, Gadi
AU - Ovadia, Michael
N1 - Funding Information:
Acknowledgemenfs-Thea uthors thank Lourival Possani (Instituto de BiotecnologiaU, niversidadN ational Autonomad e Mexico)a ndA lexandraR ucavado( InstitutoC lodomiroP icado)f or theirs upporats, w ell as Javier Nuiiez and Jorge Sanabria for skillful laboratory assistanceT. his study was supportedb y AID (Grant DHR-5544-6-00-1064-00).
PY - 1995/1
Y1 - 1995/1
N2 - A metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme has a mol. wt of 24,000 and contains few Cys and high numbers of Asp, Leu, Ser and Glu. BaP1 hydrolyzes casein, hide powder azure and fibrinogen, having an optimal pH of 8.0. It rapidly digests the Aα-chain of fibrinogen and, later on, the Bβ -chain, leaving the γ-chain unaffected. Chelating agents (EDTA and 1,10-phenanthroline) inhibited proteolytic activity, whereas 2-mercaptoethanol and soybean trypsin inhibitor did not affect this activity. BaP1 has a weak hemorrhagic activity, with a minimum hemorrhagic dose of 20 μg; this activity was inhibited by EDTA and was abolished after incubation at 60°C. In addition, BaP1 induces edema and a mild myotoxic effect, lacking coagulant, defibrinating and lethal effects.
AB - A metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme has a mol. wt of 24,000 and contains few Cys and high numbers of Asp, Leu, Ser and Glu. BaP1 hydrolyzes casein, hide powder azure and fibrinogen, having an optimal pH of 8.0. It rapidly digests the Aα-chain of fibrinogen and, later on, the Bβ -chain, leaving the γ-chain unaffected. Chelating agents (EDTA and 1,10-phenanthroline) inhibited proteolytic activity, whereas 2-mercaptoethanol and soybean trypsin inhibitor did not affect this activity. BaP1 has a weak hemorrhagic activity, with a minimum hemorrhagic dose of 20 μg; this activity was inhibited by EDTA and was abolished after incubation at 60°C. In addition, BaP1 induces edema and a mild myotoxic effect, lacking coagulant, defibrinating and lethal effects.
UR - http://www.scopus.com/inward/record.url?scp=0028924054&partnerID=8YFLogxK
U2 - 10.1016/0041-0101(94)00138-X
DO - 10.1016/0041-0101(94)00138-X
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AN - SCOPUS:0028924054
SN - 0041-0101
VL - 33
SP - 19
EP - 29
JO - Toxicon
JF - Toxicon
IS - 1
ER -