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Digitale Medien

Trypsin-catalyzed peptide synthesis withm-guanidinophenyl andm-(guanidinomethyl)phenyl esters as acyl donor component (1999)

Sekizaki, H. ; Itoh, K. ; Toyota, E. ; [weitere]

Springer

Amino acids 17 (1999), S. 285-291

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Details

ISSN: 1438-2199

Schlagwort(e): Amino acid esters ; Inverse substrate ; Kinetics of tryptic hydrolysis ; Protease catalysis ; Peptide synthesis

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01366927

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