ISSN:
0173-0835
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
A peptide amide, R-Arg-NH2, was produced by carboxypeptidase Y (CPDY)-catalyzed transpeptidation of a peptide, R-Ala-OH in presence of a large excess of Arg-NH2. Baseline separation of R-Ala-OH and R-Arg-NH2 was achieved by free solution capillary electrophoresis (CE) analysis. With CE the reactions could be closely followed with an analysis frequency of 3-6 h-1. Due to a low consumption of sample per CE analysis (1-5 nL introduced, 5-6 μL in the sample vial), the reactions were performed in 100 and 250 μL volumes. Consequently, the optimization experiments consumed limited amounts of enzyme and substrate only. At optimized experimental conditions approximately 90% conversion of the starting peptide, R-Ala-OH, to R-Arg-NH2 was achieved.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/elps.1150140175
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