| Literature DB >> 2437960 |
H Tschesche, J Beckmann, A Mehlich, E Schnabel, E Truscheit, H R Wenzel.
Abstract
A semisynthetic approach to modulate the inhibitory specificity of aprotinin, the Kunitz trypsin inhibitor from bovine mast cells, is described. By the use of peptide-chemical procedures a single amino acid of its reactive site can be replaced by any other coded or non-coded amino acid. Thus, a series of aprotinin homologues have been prepared which demonstrate the individual contribution of a single side chain to the inhibition of a particular target proteinase and enable specific inhibitors to be designed.Entities:
Mesh：
Substances：
Year: 1987 PMID： 2437960 DOI： 10.1016/0167-4838(87)90238-x
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002