Literature DB >> 14613767

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 Smoum1, Abraham Rubinstein, Morris Srebnik.   

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.

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Year:  2003        PMID： 14613767     DOI： 10.1016/j.bioorg.2003.08.004

Source DB:  PubMed          Journal:  Bioorg Chem        ISSN： 0045-2068            Impact factor:   5.275


  3 in total

1.  Random amphiphilic copolymeric sub-micro particles as a carrier shielding from enzymatic attack for peptides and proteins delivery.

Authors:  Qingyi Meng; Limin Tian; Jiaxiang Wang
Journal:  J Mater Sci Mater Med       Date:  2012-02-25       Impact factor: 3.896

2.  Potassium Boc-protected secondary aminomethyltrifluoroborates: synthesis and Suzuki-Miyaura cross-coupling reactions.

Authors:  Gary A Molander; Inji Shin
Journal:  Org Lett       Date:  2012-08-29       Impact factor: 6.005

3.  Facile synthesis of highly functionalized ethyltrifluoroborates.

Authors:  Gary A Molander; Wilma Febo-Ayala; Montserrat Ortega-Guerra
Journal:  J Org Chem       Date:  2008-06-28       Impact factor: 4.354
  3 in total

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