[The nature of differences in amidase and esterase activities of some acyltrypsins].

@article{Bresler1975TheNO,
  title={[The nature of differences in amidase and esterase activities of some acyltrypsins].},
  author={S. E. Bresler},
  journal={Biokhimiia},
  year={1975},
  volume={40 2},
  pages={408-10}
}
Specific trypsin substrates (esters, anilides, amides, peptides) were shown to accelerate deacetylation of monoacetylated trypsin. The amidase activity of monoacetyl-, monopropyonyl-, and tetraformyl-trypsin was not manifested if the amidase activity of native enzyme was suppressed in these preparations by the ester substrates (benzoylarginine ethyl ester or p-nitrophenyl acetate). Therefore the differences in the residual amidase and esterase activities of these acylated trypsin preparations… CONTINUE READING