The state of sulfhydryl groups in normal and cataractous human lens proteins. II. Cortical and nuclear regions

Experimental Eye Research

Volumn 29, Issue 3, 1979, Pages 233-243

  Anderson, E I ^a   Wright, Diane D ^a   Spector, Abraham ^a  

^a Biochemistry and Molecular Biology Laboratory Department of Ophthalmology College of Physicians and Surgeons ^*  (United States)

Author keywords

aging; cataract; disulfides; insoluble protein; lens cortex; lens nucleus; soluble protein; sulfhydryl groups

Indexed keywords

LENS PROTEIN; THIOL GROUP;

AGE; AGING; CATARACT; CATARACTOGENESIS; HUMAN; LENS CORTEX; LENS NUCLEUS; NORMAL HUMAN; VISUAL SYSTEM;

ADOLESCENT; ADULT; AGED; AGING; CATARACT; CRYSTALLINS; DISULFIDES; HUMAN; LENS, CRYSTALLINE; MIDDLE AGE; SOLUBILITY; SULFHYDRYL COMPOUNDS; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0018606203     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-4835(79)90004-6     Document Type: Article

References (11)

1. The state of sulfhydryl groups in normal and cataractous human lens proteins. 1. Nuclear region
2. Free amino acids in senile cataractous lenses: possible osmotic etiology
3. The behavior of reduced proteins from normal and cataractous lenses in highly dissociating media: crosslinked protein in cataractous lenses
4. Changes to the proteins of the human lens nucleus in cataract
5. Studies on the oxidation of cysteine to cystine in lens proteins during cataract formation
6. Glutathione and NADP linked enzymes in human senile cataract
7. Spectroscopic evaluation and classification of the normal, aging and cataractous lens
8. Colour and solubility of the proteins of human cataracts
9. Disulfide-linked high molecular weight protein associated with human cataract
10. The state of sulfhydryl groups in normal and cataractous human lenses
11. Development of non-disulfide covalent cross-links in nuclear cataractogenesis