A method for purification of peptides from hydrolysates of proteins modified by chemically active analogues of substrates containing cis-diol groups.
A simple and rapid column procedure is described for the isolation from protein hydrolysates of peptides containing covalently bound substrate analogues with cis-diol groups. The method is based on complex formation between the cis-diol groups of peptide-bound compounds and dihydroxyborylic groups of a dihydroxyborylaminoethyl cellulose column. The method is useful for isolation of peptide(s) located in or near the active centre of enzymes after their affinity labelling by chemically active analogues of natural substrates like ribonucleotides, sugars, etc.
D000255:Adenosine Triphosphate; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002846:Chromatography, Affinity / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D010446:Peptide Fragments / Q000302:isolation & purification*; D012265:Ribonucleotides / Q000378:metabolism; D012266:Ribose / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D010446:Peptide Fragments; D012265:Ribonucleotides; D012266:Ribose; D000255:Adenosine Triphosphate