TY - JOUR
T1 - Inhibition of the proteolytic activity of hemorrhagin-e from Crotalus atrox venom by antihemorrhagins from homologous serum
AU - Weissenberg, Sarah
AU - Ovadia, Michael
AU - Kochva, Elazar
N1 - Funding Information:
Acknowledgements--We thank Prof. A. BDOLAHf or reading the manuscript and for many useful remarks. This work was supported in part by a grant from the Basic Research Foundation of Tel-Aviv University (M.O.) and by the Rose and Norman Lederer Chair in Experimental Biology (E.K.).
PY - 1992
Y1 - 1992
N2 - Antihemorrhagic proteins from Crotalus atrox serum were tested for their ability to inhibit the proteolytic activity of the hemorrhagic toxin-e from Crotalus atrox venom and of several other proteolytic enzymes: trypsin, collagenase and thermolysin. The antihemorrhagic proteins inhibited the proteolytic activity of hemorrhagin-e when tested on gelatin type I and collagen type IV, the proteolytic activity of trypsin on photofilm gelatin and the proteolytic activity of whole venom when tested on azocollagen and photofilm gelatin. The antihemorrhagins failed to inhibit the proteolytic activity of trypsin when tested on the specific synthetic substrate N-acetyl-dl-phenylalanine-β-naphthyl ester (APNE), the activity of microbial collagenase on N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala (FALGPA) or on azocollagen and the activity of thermolysin on N-(3-[2-furyl] acryloyl)-Gly-Leu amide (FAGLA). It is tentatively suggested that the antihemorrhagins from snake blood serum are proteinase inhibitors that under-went specialization towards the neutralization of the proteolytic activity of hemorrhagic toxins.
AB - Antihemorrhagic proteins from Crotalus atrox serum were tested for their ability to inhibit the proteolytic activity of the hemorrhagic toxin-e from Crotalus atrox venom and of several other proteolytic enzymes: trypsin, collagenase and thermolysin. The antihemorrhagic proteins inhibited the proteolytic activity of hemorrhagin-e when tested on gelatin type I and collagen type IV, the proteolytic activity of trypsin on photofilm gelatin and the proteolytic activity of whole venom when tested on azocollagen and photofilm gelatin. The antihemorrhagins failed to inhibit the proteolytic activity of trypsin when tested on the specific synthetic substrate N-acetyl-dl-phenylalanine-β-naphthyl ester (APNE), the activity of microbial collagenase on N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala (FALGPA) or on azocollagen and the activity of thermolysin on N-(3-[2-furyl] acryloyl)-Gly-Leu amide (FAGLA). It is tentatively suggested that the antihemorrhagins from snake blood serum are proteinase inhibitors that under-went specialization towards the neutralization of the proteolytic activity of hemorrhagic toxins.
UR - http://www.scopus.com/inward/record.url?scp=0026643167&partnerID=8YFLogxK
U2 - 10.1016/0041-0101(92)90853-W
DO - 10.1016/0041-0101(92)90853-W
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AN - SCOPUS:0026643167
SN - 0041-0101
VL - 30
SP - 591
EP - 597
JO - Toxicon
JF - Toxicon
IS - 5-6
ER -