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The primary structure of crotalase a thrombin like venom enzyme exhibits closer homology to kallikrein than to other serine proteases


, : The primary structure of crotalase a thrombin like venom enzyme exhibits closer homology to kallikrein than to other serine proteases. Biochemical & Biophysical Research Communications 99(2): 715-721

Amino acid sequences of [Crotalus adamanteus] crotalase, totaling 98 residues or about 37% of the molecule, were determined by Edman degradation and compared with the published sequences of 9 serine proteases. Homologous alignment could be found for all crotalase sequences except 1 decapeptide. Comparison between crotalase and procine pancreatic kallikrein showed the largest number of identical amino acids (36%). This finding has led to experiments which demonstrate that crotalase has specific enzymatic properties resembling kallikrein.

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Accession: 006740884

PMID: 7016120

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Related references

Pirkle H.; Markland F.S.; Bajwa S.S.; Theodor I.; Baumgartner R.; Kirakossian H., 1981: The primary structure of crotalase a thrombin like venom enzyme exhibits strong homology with kallikrein. Thrombosis & Haemostasis 46(1): 46

Henschen-Edman, A.H.; Theodor, I.; Edwards, B.F.; Pirkle, H., 1999: Crotalase, a fibrinogen-clotting snake venom enzyme: primary structure and evidence for a fibrinogen recognition exosite different from thrombin. Crotalase, a fibrinogen-clotting enzyme isolated from the venom of Crotalus adamanteus, and its overlapping fragments were subjected to Edman degradation. The resulting amino acid sequence, VIGGDEC NINEHRFLVALYDYWSQLFLCGGTLINNEWVLTAAHCDRTHI LIYVGV...

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