Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme

FEBS Letters

Volumn 398, Issue 2-3, 1996, Pages 322-325

  Sjöblom, Björn ^a   Elleby, Björn ^a   Wallgren, Katarina ^a   Jonsson, Bengt Harald ^a   Lindskog, Sven ^a  

^a UMEÅ UNIVERSITY   (Sweden)

Author keywords

Acetazolamide; Carbonic anhydrase related protein; CO2 hydration; Mutagenesis; Zinc binding

Indexed keywords

ACETAZOLAMIDE; CARBONATE DEHYDRATASE;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; BRAIN; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; MOLECULAR WEIGHT; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION;

ACETAZOLAMIDE; AMINO ACID SEQUENCE; ANIMALS; CARBON DIOXIDE; CARBONIC ANHYDRASE INHIBITORS; CARBONIC ANHYDRASES; DNA, COMPLEMENTARY; MICE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; POINT MUTATION; RECOMBINANT PROTEINS; ZINC;

ANIMALIA; CYPRINUS CARPIO; ESCHERICHIA COLI; MAMMALIA; MURINAE;

EID: 0030566855     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(96)01263-X     Document Type: Article

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