Abstract
Hydrolysis of two general proteinase substrates and seven substrates specific for trypsin-like and chymotrypsin-like enzymes, aminopeptidases, and carboxypeptidases was demonstrated by homogenates of alimentary systems of larvae and adults of Sitophilus oryzae (L.), S. zeamais Motchulsky, and S. granarius (L.). Endopeptidase activity was very low in all species, whereas aminopeptidases and carboxypeptidases were relatively active. Hydrolysis of α-N-benzoyl-DL-arginine-p-nitroanilide (BApNA) by larvae and adults of S. granarius was due to a single enzyme, inhibited by N-α-tosyl-L-lysinechloromethyl ketone (TLCK) and soybean trypsin inhibitor, and with a relative mobility of 0.49 on an anionic polyacrylamide gel system. This enzyme was not detected in S. oryzae or S. zeamais. Aminopeptidases (hydrolysis of L-leucine-p-nitroanilide) were inhibited by 1, 10-phenanthroline, Cd2+, and Hg2+, and existed in two major and two to three minor isozymes in each species. Water extracts of wheat and corn flour inhibited the BApNA enzyme from S. granarius but had no effect upon the aminopeptidases and carboxypeptidases (hydrolysis of N-carbobenzoxy-L-valyl-L-leucine).
Publisher
Canadian Science Publishing
Subject
Animal Science and Zoology,Ecology, Evolution, Behavior and Systematics
Cited by
45 articles.
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