Proteins or peptides having an \(\mathrm{N}\)-terminal-blocked amino acid were successively digested by pronase \(E\), proteinase \(K\), and carboxypeptidase \(Y\). The \(\mathbf{N}\)-blocked amino acids released from proteins or peptides were derivatized with 9 -anthryldiazomethane (ADAM) to the co
Enzymic cleavage of the blocked amino terminal residues of peptides
โ Scribed by Wanda M. Jones; Lois R. Manning; James M. Manning
- Book ID
- 117056930
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 306 KB
- Volume
- 139
- Category
- Article
- ISSN
- 0006-291X
No coin nor oath required. For personal study only.
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A method for selective isolation of the amino \(\mathrm{N}\)-terminal peptide from an \(\alpha\)-amino \(\left(N^{\alpha}\right.\) )-blocked protein is presented. The method consists of four steps. First, \(\epsilon-\) amino groups of lysine residues in the protein are succinylated. Second, the deri