The application of papain, ficin and clostripain in kinetically controlled peptide synthesis in frozen aqueous solutions
✍ Scribed by Dr Marion Hänsler; Grit Ullmann; Hans-Dieter Jakubke
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 398 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1075-2617
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The capability of the cysteine proteases ficin, papain and clostripain to form peptide bonds in frozen aqueous solutions was investigated. Freezing the reaction mixture resulted in increased peptide yields in kinetically controlled coupling of Bz–Arg–OEt with various amino acid amides and dipeptides. Under these conditions, peptide yields increased up to 70% depending on the enzyme and the amino component used. Enzyme‐catalysed peptide syntheses were carried out under optimized reaction conditions (temperature, amino component concentration and pH before freezing) using the condensation of Bz–Arg–OEt and H–Leu–NH~2~ as a model reaction.
📜 SIMILAR VOLUMES
## Abstract Glycine in aqueous solutions of trimetaphosphate or linear polyphosphate at pH adjusted to 8.1‐9.0, is condensed at room temperature to diglycine and very small amounts of triglycine. The addition of imidazole increases the yield of triglycine by a factor of almost 10; supplementary add