[Affinity chromatography of aminopeptidases].
The recent data are generalized concerning a series of synthetic oligopeptides which are competitive inhibitors of aminopeptidases of animal, plant and microbic origin. A method for biospecific chromatography of these enzymes is developed, using as ligands such inhibitors as diazo derivatives of p-aminophenyl-, chloromethyl- and methylketones of L-amino acids and peptides, amino acids, aliphatic acid amides. It is established that the most effective inhibitors of aminopeptidases contain L-amino group in the uncharged form in the N-end position, hydrophobic lateral chain of L-configuration and a carbonyl group analogous to position of these groups in the substrate. Methods for synthesis of certain peptides are developed with respect to the above requirements. It is shown that peptides with a space-inaccessible peptide link and antibiotics are often used as ligands for affinity chromatography of aminopeptidases. At present a nonspecific (ion-exchange, hydrophobic) interaction of sorbent and aminopeptidases is observed, which necessitates to increase the specificity at the stage of the enzyme desorption in the further studies.
D000333:Aeromonas / Q000201:enzymology; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D001236:Aspergillus oryzae / Q000201:enzymology; D002846:Chromatography, Affinity / Q000379:methods; D003013:Clostridium / Q000201:enzymology; D007700:Kinetics; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D000626:Aminopeptidases
Affinnaia khromatografiia aminopeptidaz.