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
β¦ LIBER β¦
Solid phase synthesis of peptides with polyethylene glycol-modified protease in organic solvents
β Scribed by K. Sakurai; K. Kashimoto; Y. Kodera; Y. Inada
- Publisher
- Springer Netherlands
- Year
- 1990
- Tongue
- English
- Weight
- 271 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0141-5492
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## Abstract This manuscript shows that ACN can be an excellent choice for the coupling of hindered amino acids as illustrated by the coupling of Fmocβamino acids on free amino acids anchored on a BAL synthesis. Furthermore, ACN can be a good alternative for solidβphase peptide synthesis in the abse