VTechWorks is currently accessible only on the VT network (campus, VPN). Elements deposit is now enabled. We are working to restore full access as soon as possible.
 

Alkylation of rat lens crystallins with iodoacetamide

TR Number

Date

1977-09-05

Journal Title

Journal ISSN

Volume Title

Publisher

Virginia Tech

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.

Description

Keywords

Citation

Collections