Peptide synthesis catalyzed by the serine proteinases chymotrypsin and trypsin
โ Scribed by Lutz Riechmann; Volker Kasche
- Book ID
- 113265799
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 585 KB
- Volume
- 830
- Category
- Article
- ISSN
- 0167-4838
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Chymotrypsin modified with polyethylene glycol was successfully used for peptide synthesis in organic solvents. The benzene-soluble modified enzyme readily catalyzed both aminolysis of N-benzoyl-L-tyrosine p-nitroanilide and synthesis of N-benzoyl-L-tyrosine butylamide in the presence of trace amoun
Benzyloxycarbonyl-L-proline p-guanidinophenyl ester is an "inverse substrate" for trypsin; i.e., the cationic center is included in the leaving group instead of being in the acyl moiety. This substrate can be used in trypsin-catalyzed acyl-transfer reactions leading to the sythesis of Pro-Xaa peptid