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. / Master of Science
| Identifer | oai:union.ndltd.org:VTETD/oai:vtechworks.lib.vt.edu:10919/43951 |
| Date | 28 July 2010 |
| Creators | Haynes, Linda Rose |
| Contributors | Biochemistry and Nutrition, Hess, John L., Barnett, Lewis B., Bunce, George Edwin, Rutherford, Charles L. |
| Publisher | Virginia Tech |
| Source Sets | Virginia Tech Theses and Dissertation |
| Language | English |
| Detected Language | English |
| Type | Thesis, Text |
| Format | 73 leaves, BTD, application/pdf, application/pdf |
| Rights | In Copyright, http://rightsstatements.org/vocab/InC/1.0/ |
| Relation | OCLC# 21387698, LD5655.V855_1977.H39.pdf |
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