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Volumn 93, Issue 24, 1996, Pages 13647-13652
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Gly-63 → Gln substitution adjacent to His-64 in rodent carbonic anhydrase IVs largely explains their reduced activity
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Author keywords
[No Author keywords available]
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Indexed keywords
CARBONATE DEHYDRATASE;
GLYCINE;
HISTIDINE;
GLUTAMINE;
ISOENZYME;
RECOMBINANT PROTEIN;
AMINO ACID SUBSTITUTION;
ANIMAL CELL;
CHEMICAL REACTION KINETICS;
CONFERENCE PAPER;
ENDOTHELIUM CELL;
ENZYME PURIFICATION;
HUMAN;
HUMAN CELL;
MOLECULAR DYNAMICS;
MOUSE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTON TRANSPORT;
RAT;
AMINO ACID SEQUENCE;
ANIMAL;
ARTICLE;
CATTLE;
CELL MEMBRANE;
CELL STRAIN COS1;
CHEMISTRY;
COMPARATIVE STUDY;
ENZYMOLOGY;
GENE LIBRARY;
GENETIC TRANSFECTION;
KIDNEY;
KINETICS;
LUNG;
METABOLISM;
MOLECULAR GENETICS;
NUCLEOTIDE SEQUENCE;
POINT MUTATION;
RABBIT;
SEQUENCE HOMOLOGY;
SITE DIRECTED MUTAGENESIS;
ANIMALIA;
BOVINAE;
MURINAE;
ORYCTOLAGUS CUNICULUS;
RODENTIA;
AMINO ACID SEQUENCE;
ANIMALS;
BASE SEQUENCE;
CARBONIC ANHYDRASES;
CATTLE;
CELL MEMBRANE;
COS CELLS;
GENE LIBRARY;
GLUTAMINE;
GLYCINE;
HISTIDINE;
HUMANS;
ISOENZYMES;
KIDNEY;
KINETICS;
LUNG;
MICE;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
POINT MUTATION;
RABBITS;
RATS;
RECOMBINANT PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
TRANSFECTION;
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EID: 0030300131
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.93.24.13647 Document Type: Article |
Times cited : (22)
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References (35)
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