Determination of anti-protease homogeneity.
Virgin and modified [single peptide bond between arginine (63) and isoleucine (64) is cleaved] soybean anti-trypsin was separated by chromatofocusing using a narrow pH range. The separation on anion-exchange and reversed-phase chromatography was less satisfactory. Anti-proteases isolated by affinity chromatography from Boophilus decoloratus were monitored for the formation of any modified protein, with chromatofocusing.
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D011480:Protease Inhibitors / Q000032:analysis*; D013987:Ticks / Q000201:enzymology; D014118:Toxins, Biological / Q000032:analysis; D014361:Trypsin Inhibitors / Q000032:analysis / Q000302:isolation & purification
D011480:Protease Inhibitors; D014118:Toxins, Biological; D014361:Trypsin Inhibitors