ISSN:
1438-2199
Keywords:
Amino acid esters
;
Inverse substrate
;
Kinetics of tryptic hydrolysis
;
Protease catalysis
;
Peptide synthesis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Summary Two series of inverse substrates,m-guanidinophenyl andm-(guanidinomethyl)phenyl esters derived fromN-(tert-butyloxycarbonyl)amino acid, were prepared as an acyl donor component for trypsin-catalyzed peptide synthesis. The kinetic behavior of these esters toward tryptic hydrolysis was analyzed. They were found to couple with an acyl acceptor such asl-alaninep-nitroanilide to produce dipeptide in the presence of trypsin.Streptomyces griseus trypsin was a more efficient catalyst than the bovine trypsin. Within the enzymatic peptide coupling methods, this approach was shown to be advantageous, since the resulting peptides are resistant to the enzymatic hydrolysis.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01366927
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