Corpus ID: 31169838

Synthesis and hydrolysis by arginyl-hydrolases of p-nitroanilide chromogenic substrates containing polyethylene glycol and D-gluconyl moieties.

@article{Juliano1991SynthesisAH,
  title={Synthesis and hydrolysis by arginyl-hydrolases of p-nitroanilide chromogenic substrates containing polyethylene glycol and D-gluconyl moieties.},
  author={Maria Aparecida Juliano and Luiz Juliano and Laura Biondi and Raniero Rocchi},
  journal={Peptide research},
  year={1991},
  volume={4 6},
  pages={
          334-9
        }
}
D-Gluconic acid and alpha-carboxymethyl-polyethylene-glycol-omega-methyl ether (PEG) (mol wt 550) were covalently bound at N alpha-amino group of H-Phe-Arg-pNa to study the effect on hydrolysis by arginyl-hydrolases of chromogenic substrates containing high hydrophilic and amphiphilic groups. For comparison, epsilon-aminocaproyl-, sarcosyl- and succinyl-Phe-Arg-pNa were also synthesized. The obtained compounds were assayed as substrates for porcine pancreatic kallikrein, horse urinary… Expand
1 Citations
Chromogenic and fluorogenic glycosylated and acetylglycosylated peptides as substrates for serine, thiol and aspartyl proteases.
TLDR
The acetylation of sugar hydroxyl groups improved hydrolysis of the susceptible peptides to all enzymes, except tonin, and human cathepsin D and porcine pepsin are more tolerant to substrate glycosylation, hydrolysing both the P'4 and P4 gly cosylated substrates. Expand