[Preparation and characteristics of carboxymethylated lysozyme derivatives].
Hen egg-white lysozyme (EC 3.2.1.17) was carboxymethylated with iodoacetic acid and the individual products of various degree of modification were isolated by column chromatography on Amberlite CG-50. Peptide mapping of the products obtained reveals that His-15, Lys-1, -33, -96 (or -97) residues are blocked; the Lys-13 and -116 residues are unmodified. Salt activation of the carboxymethylated derivatives is facilitated with the increase of the number of modified groups; this fact is consistent with the increased lytic activity and affinity to substrate of the derivatives at lowered ionic strength.
D002852:Chromatography, Ion Exchange; D006639:Histidine / Q000031:analogs & derivatives; D007461:Iodoacetates; D008239:Lysine / Q000031:analogs & derivatives; D008745:Methylation; D009113:Muramidase / Q000378:metabolism*; D009994:Osmolar Concentration
D007461:Iodoacetates; D006639:Histidine; D009113:Muramidase; D008239:Lysine
Poluchenie i kharakteristika karboksimetilproizvodnykh lizotsima.