A study of the effect on nucleophilic hydrolytic activity of pancreatic elastase, trypsin, chymotrypsin, and leucine aminopeptidase by boronic acids in the presence of arabinogalactan: A subsequent study on the hydrolytic activity of chymotrypsin by boronic acids in the presence of mono-, di-, and trisaccharides

Reem Smoum, Abraham Rubinstein*, Morris Srebnik

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

The hydrolytic activity of trypsin, chymotrypsin, elastase, and leucine aminopeptidase, is inhibited by different boronic acids. However, all the enzymes are inhibited by the compound CbzAla(boro)Gly(OH)2. Therefore, these additives can control the nucleophilic hydrolytic activity of these enzymes.

Original languageAmerican English
Pages (from-to)464-474
Number of pages11
JournalBioorganic Chemistry
Volume31
Issue number6
DOIs
StatePublished - Dec 2003

Bibliographical note

Funding Information:
This project was supported by a grant from the Israeli Science Foundation Grant No. 663/99-2.

Keywords

  • Boronic acids
  • Hydrolytic activity
  • Inhibition
  • Saccharides
  • Serine proteases

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