γIII-Crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions

Biochemical Journal

Volumn 374, Issue 3, 2003, Pages 677-685

  Yan, Hong ^a,b   Willis, Antony C ^a   Harding, John J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b FOURTH MILITARY MEDICAL UNIVERSITY   (China)

Author keywords

Cataract; Fructose; Glucose; Glycation; Lens; Post translational modification

Indexed keywords

PROTEINS; REACTION KINETICS; SIZE EXCLUSION CHROMATOGRAPHY; SUGARS;

GLYCATION;

PHYSIOLOGY;

ALPHA CRYSTALLIN; BETA CRYSTALLIN; FRUCTOSE; GAMMA CRYSTALLIN; GLUCOSE; PROTEIN SUBUNIT; TISSUE CULTURE MEDIUM; TRYPSIN; CARBON;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CATTLE; CONTROLLED STUDY; GEL PERMEATION CHROMATOGRAPHY; ISOTOPE LABELING; LENS; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN GLYCOSYLATION; PROTEIN ISOLATION; PROTEIN SECRETION; ANIMAL; CHEMISTRY; GLYCOSYLATION; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; SEQUENCE ANALYSIS;

ANIMALIA; BOS TAURUS; BOVINAE;

AMINO ACID SEQUENCE; ANIMALS; CARBON RADIOISOTOPES; CATTLE; FRUCTOSE; GAMMA-CRYSTALLINS; GLUCOSE; GLYCOSYLATION; LENS, CRYSTALLINE; MOLECULAR SEQUENCE DATA; SEQUENCE ANALYSIS, PROTEIN;

EID: 0141609687     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030542     Document Type: Article

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