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Alkylation of rat lens crystallins with iodoacetamide
Alkylation of lens proteins with iodoacetamide during homogenization of tissue (50 millimolar excess) immediately followed by gel-permeation chromatography yielded a crystallin population devoid of Î²H-crystallin. This result occurred in lens homogenates from both young (100 g) and older (400 g) male rats. BetaH-crystallin was not converted to insoluble protein with alkylation. Each crystallin fraction reacted with radioactive iodoacetamide in proportion to sulfhydryl content; at a ratio of 1 mg iodoacetamide/mg protein total free-sulfhydryl of the crystallins had reacted after 1 hr at pH 8, 25Â°C. Alkylated Î±-, Î²L-' and y-crystallin fractions demonstrated no altered chromatographic behavior on Sephacryl S-200; only alkylated Î²H-crystallin was altered so that it co-chromatographed with control or alkylated Î²L-crystallin.