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Separation and Partial Characterization of a Coagulant Enzyme from Bitis gabonica Venom
Author(s) -
Marsh N. A.,
Whaler B. C.
Publication year - 1974
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1974.tb00474.x
Subject(s) - venom , size exclusion chromatography , chemistry , chromatography , fibrinogen , ion chromatography , proteolytic enzymes , enzyme , biochemistry
S ummary . The venom of the Gaboon viper ( Bitis gabonica ) has been shown to possess both coagulant and anticoagulant activities in vitro. These findings confirm in part previous results, the latter effect probably being achieved by proteolytic breakdown of fibrinogen. A partially purified coagulant has been recovered by ion‐exchange chromatography and gel filtration. Initial results indicate that this material may be similar in some respects to ancrod and reptilase. Anaesthetized rabbits were totally defibrinated without any apparent short‐term deleterious effects.