sepharose has been researched along with 4-nitrophenyl-acetate* in 1 studies
1 other study(ies) available for sepharose and 4-nitrophenyl-acetate
| Article | Year |
|---|---|
Thiolsubtilisin as an instrument for peptide synthesis. Preparation and properties.
A convenient procedure for thiolsubtilisin purification from an admixture of subtilisin involving affinity chromatography on bacitracin-Sepharose is presented. Thiolsubtilisin activity was measured by hydrolysis of p-nitrophenyl acetate, p-nitroanilide-peptide (Glp-Ala-Ala-Leu-pNA), and azocasein. The thiolenzyme catalyzes peptide synthesis. Under these conditions only activated peptide esters, e.g., p-chlorophenyl, N-hydroxysuccinimide, or p-nitrophenyl esters form peptide bonds during interaction with appropriate nucleophiles such as peptides and their derivatives and amino acid amides. Topics: Amino Acids; Bacillus subtilis; Bacitracin; Caseins; Chromatography, Affinity; Chromatography, Gel; Hydrolysis; Nitrophenols; Peptide Biosynthesis; Peptides; Sepharose; Substrate Specificity; Subtilisins | 1997 |