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Volumn 413, Issue 2, 1997, Pages 339-343
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The catalytic domain of dihydrolipoyl acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Expression, purification and reversible denaturation
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Author keywords
Catalytic domain; Chaperonin; Dihydrolipoyl acetyltransferase; Multienzyme complex; Reversible denaturation; Self assembly
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Indexed keywords
DIHYDROLIPOAMIDE ACETYLTRANSFERASE;
PYRUVATE DEHYDROGENASE;
ARTICLE;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME PURIFICATION;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
GEOBACILLUS STEAROTHERMOPHILUS;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
ACETYL COENZYME A;
ACETYLTRANSFERASES;
BACILLUS STEAROTHERMOPHILUS;
CATALYSIS;
DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE;
ESCHERICHIA COLI;
GUANIDINE;
GUANIDINES;
KINETICS;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PYRUVATE DEHYDROGENASE COMPLEX;
RECOMBINANT FUSION PROTEINS;
THIOCTIC ACID;
ESCHERICHIA COLI;
GEOBACILLUS STEAROTHERMOPHILUS;
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EID: 0030758675
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(97)00932-0 Document Type: Article |
Times cited : (35)
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References (28)
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