An investigation of the coagulogical potential of the venoms of some Central Asian snakes

L. Ya. Yukel'son; E.S. Sadykov; N.A. Barabanshchikova; J. Rosing; Guido Tans; H.C. Hemker

doi:10.1007/BF00630546

An investigation of the coagulogical potential of the venoms of some Central Asian snakes

L. Ya. Yukel'son, E.S. Sadykov, N.A. Barabanshchikova, J. Rosing, Guido Tans, H.C. Hemker

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Abstract

The compositions of the proteolytic complexes of the venoms of the crotalid agkistrodon halys halysand the viperid echis multisquamatushave been investigated with the aid of a large number of specific natural and model substrates. A comparative analysis of the results obtained has revealed a predominance in the crotalid venom of fibrinogen-hydrolyzing enzymes, while the viperid venom is characterized as a procoagulant of the prothrombin-activating type. Among the fibrinogenases of the crotalid venom, a thrombin-like enzyme and a plasmin-like proteinase have been revealed and obtained in a purified state. A prothrombin-activating enzyme from the viperid venom has been isolated in the purified state and characterized with the aid of specific substrates.

Original language	English
Pages (from-to)	384-390
Number of pages	7
Journal	Chemistry of Natural Compounds
Volume	29
Issue number	3
DOIs	https://doi.org/10.1007/BF00630546
Publication status	Published - 1993

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title = "An investigation of the coagulogical potential of the venoms of some Central Asian snakes",

abstract = "The compositions of the proteolytic complexes of the venoms of the crotalid agkistrodon halys halysand the viperid echis multisquamatushave been investigated with the aid of a large number of specific natural and model substrates. A comparative analysis of the results obtained has revealed a predominance in the crotalid venom of fibrinogen-hydrolyzing enzymes, while the viperid venom is characterized as a procoagulant of the prothrombin-activating type. Among the fibrinogenases of the crotalid venom, a thrombin-like enzyme and a plasmin-like proteinase have been revealed and obtained in a purified state. A prothrombin-activating enzyme from the viperid venom has been isolated in the purified state and characterized with the aid of specific substrates.",

author = "Yukel'son, {L. Ya.} and E.S. Sadykov and N.A. Barabanshchikova and J. Rosing and Guido Tans and H.C. Hemker",

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journal = "Chemistry of Natural Compounds",

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TY - JOUR

T1 - An investigation of the coagulogical potential of the venoms of some Central Asian snakes

AU - Yukel'son, L. Ya.

AU - Sadykov, E.S.

AU - Barabanshchikova, N.A.

AU - Rosing, J.

AU - Tans, Guido

AU - Hemker, H.C.

PY - 1993

Y1 - 1993

N2 - The compositions of the proteolytic complexes of the venoms of the crotalid agkistrodon halys halysand the viperid echis multisquamatushave been investigated with the aid of a large number of specific natural and model substrates. A comparative analysis of the results obtained has revealed a predominance in the crotalid venom of fibrinogen-hydrolyzing enzymes, while the viperid venom is characterized as a procoagulant of the prothrombin-activating type. Among the fibrinogenases of the crotalid venom, a thrombin-like enzyme and a plasmin-like proteinase have been revealed and obtained in a purified state. A prothrombin-activating enzyme from the viperid venom has been isolated in the purified state and characterized with the aid of specific substrates.

AB - The compositions of the proteolytic complexes of the venoms of the crotalid agkistrodon halys halysand the viperid echis multisquamatushave been investigated with the aid of a large number of specific natural and model substrates. A comparative analysis of the results obtained has revealed a predominance in the crotalid venom of fibrinogen-hydrolyzing enzymes, while the viperid venom is characterized as a procoagulant of the prothrombin-activating type. Among the fibrinogenases of the crotalid venom, a thrombin-like enzyme and a plasmin-like proteinase have been revealed and obtained in a purified state. A prothrombin-activating enzyme from the viperid venom has been isolated in the purified state and characterized with the aid of specific substrates.

U2 - 10.1007/BF00630546

DO - 10.1007/BF00630546

M3 - Article

SN - 0009-3130

VL - 29

SP - 384

EP - 390

JO - Chemistry of Natural Compounds

JF - Chemistry of Natural Compounds

IS - 3

ER -