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Volumn 41, Issue 10, 2002, Pages 3329-3340
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Diverse stability and catalytic properties of human tryptase α and β isoforms are mediated by residue differences at the S1 pocket
a
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Author keywords
[No Author keywords available]
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Indexed keywords
CIRCULAR DICHROISMS (CDS);
MUTATIONS;
CATALYST ACTIVITY;
MUTAGENESIS;
PHYSIOLOGY;
SIZE EXCLUSION CHROMATOGRAPHY;
SKIN;
ENZYMES;
ASPARTIC ACID;
CHYMOTRYPSINOGEN;
ENZYME INHIBITOR;
ENZYME VARIANT;
ISOENZYME;
RECOMBINANT ENZYME;
SODIUM CHLORIDE;
TETRAMER;
TRYPTASE;
TRYPTASE ALPHA;
TRYPTASE BETA;
UNCLASSIFIED DRUG;
ARTICLE;
CATALYSIS;
CIRCULAR DICHROISM;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME INACTIVATION;
ENZYME SPECIFICITY;
ENZYME STABILITY;
ENZYME STRUCTURE;
FLUORESCENCE SPECTROSCOPY;
GEL PERMEATION CHROMATOGRAPHY;
HUMAN;
HYDROLYSIS;
INDUCED MUTATION;
PRIORITY JOURNAL;
AMINO ACID SEQUENCE;
BASE SEQUENCE;
CATALYSIS;
CIRCULAR DICHROISM;
DNA PRIMERS;
ENZYME STABILITY;
HUMANS;
ISOENZYMES;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN CONFORMATION;
SEQUENCE HOMOLOGY, AMINO ACID;
SERINE ENDOPEPTIDASES;
TRYPTASES;
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EID: 0037066138
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi015662v Document Type: Article |
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Times cited : (35)
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References (44)
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