HYDROLYSIS OF PEPTIDES BY SNAKE VENOMS OF AUSTRALIA AND NEW GUINEA

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Abstract
Summary: Peptidase substrate specificities of 9 venoms of poisonous snakes of Australia and New Guinea were investigated. Thirty‐four peptides (29 dipeptides and 5 tripeptides) were used as substrates. The peptides Gly‐L‐Asp, Gly‐L‐Glu, Gly‐L‐Pro, L‐Leu‐L‐Phe, DL‐Leu‐DL‐Val, L‐Lys‐Gly, and L‐Pro‐Gly were not hydrolyzed by any of the venoms. All other dipeptides with the exception of L‐Phe‐L‐Phe were hydrolyzed by all of the venoms investigated. Although the glycylphenylalanine linkage of the tripeptide Gly‐L‐Phe‐L‐Phe Was hydrolyzed by each of the venoms investigated, the phenylalanyl‐phenylalanie bond was only split by the venoms of N. scutatus scutatus, O. scutellatus scutellatus, and O. scutellatus canni. In like manner, L‐Phe‐L‐Phe was also hydrolyzed only by the venoms of N. scutatus scutatus, O. scutellatus canni, and O. scutellatus scutellatus.