The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 9, 1996, Pages 4170-4174

  Cabiscol, Elisa ^a,c   Levine, Rodney L ^a,b  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c GENERALITAT DE CATALUNYA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE III; PHOSPHATASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; COVALENT BOND; DISULFIDE BOND; ENZYME BINDING; ENZYME PURIFICATION; ENZYME REGULATION; ENZYME STRUCTURE; MALE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; RAT;

AMINO ACID SEQUENCE; ANIMALS; CARBONIC ANHYDRASES; CYSTEINE; FLUORESCEINS; FLUORESCENT DYES; GLUTATHIONE; HUMANS; ISOENZYMES; KINETICS; MALE; MOLECULAR SEQUENCE DATA; PHOSPHOPEPTIDES; PROTEIN-TYROSINE KINASES; PROTEIN-TYROSINE-PHOSPHATASE; RATS; RATS, INBRED F344; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0030008246     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.9.4170     Document Type: Article

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