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


Accession: 006740884

PMID: 7016120



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