A radiometric assay for studying the proteolytic activity of endopeptidases using a radiolabeled biotinyl peptide substrate is described. The method relies on the use of a peptidyl substrate incorporating susceptible bonds located between a biotinyl group at one end and a radioiodinated group at the
Enzymes as reagents in the synthesis of peptides
β Scribed by John D. Glass
- Book ID
- 107888654
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 736 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0141-0229
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π SIMILAR VOLUMES
A new C-4 chiral building block, that is a tn> (hydroxymethyl)methane derivative where the three equivalent hydroxymethyl groups have been differentiated [(THYM)\*], was prepared with excellent enautioselection, through PPL catalysed monohydrolysis of prochiral diacetate 3.
In this paper, the literature of the past few years on the application of the proteolytic enzymes in peptide synthesis is summarized. The principle is sound and peptide synthesis for commercial purposes appears feasible. The exclusion of water or its use at a low concentration in immiscible or in bi