Design of novel affinity adsorbents for the purification of trypsin‐like proteases
- 1 June 1992
- journal article
- research article
- Published by Wiley in Journal of Molecular Recognition
- Vol. 5 (2) , 55-68
Abstract
A number of ligands for the selective purification by affinity chromatography of the trypsin‐like protease, porcine pancreatic kallikrein, were designedde novoby computer‐aided molecular design. The ligands were designed to mimic the side‐chains of a number of arginyl dipeptides and included a benzamidine moiety substituted on a triazine ring. The ligands displayed inhibitory activities against pancreatic kallikrein which mirrored the specificity constants of the dipeptides they were designed to mimic. The ligand with the highest affinity for the enzyme, and analogue of a Phe‐Arg dipeptide, when immobilized to Sepharose CL‐4B via a hexamethylene spacer arm, purified pancreatic kallikrein 110‐fold in one step from a crude pancreatic acetone extract.Keywords
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