Methylation of histidine-57 in alpha-chymotrypsin by methyl p-nitrobenzenesulfonate. A new approach to enzyme modification.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002247:Carbon Isotopes; D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D002854:Chromatography, Paper; D002918:Chymotrypsin / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D002934:Cinnamates; D004355:Drug Stability; D004586:Electrophoresis; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles; D007700:Kinetics; D008722:Methods; D008745:Methylation; D009578:Nitrobenzenes; D010455:Peptides / Q000032:analysis; D011480:Protease Inhibitors; D013053:Spectrophotometry; D013451:Sulfonic Acids; D013552:Swine; D014361:Trypsin Inhibitors; D014364:Tryptophan; D014466:Ultraviolet Rays
D000596:Amino Acids; D002247:Carbon Isotopes; D002934:Cinnamates; D007093:Imidazoles; D009578:Nitrobenzenes; D010455:Peptides; D011480:Protease Inhibitors; D013451:Sulfonic Acids; D014361:Trypsin Inhibitors; D006639:Histidine; D014364:Tryptophan; D002918:Chymotrypsin