Type of Document	Master's Thesis
Author	Haynes, Linda Rose
URN	etd-07282010-020246
Title	Alkylation of rat lens crystallins with iodoacetamide
Degree	Master of Science
Department	Biochemistry and Nutrition
Advisory Committee	Advisor Name Title Hess, John L. Committee Chair Barnett, Lewis B. Committee Member Bunce, George Edwin Committee Member Rutherford, Charles L. Committee Member
Keywords	Alkylation
Date of Defense	1977-09-05
Availability	restricted
Abstract 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 βH-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, 25°C. Alkylated α-, βL-' and y-crystallin fractions demonstrated no altered chromatographic behavior on Sephacryl S-200; only alkylated βH-crystallin was altered so that it co-chromatographed with control or alkylated βL-crystallin.
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