A fragment consisting of the first 204 amino-terminal amino acids of human arylamine N-acetyltransferase one (NAT1) and the first transacetylation step of catalysis

Biochemical Pharmacology

Volumn 53, Issue 1, 1997, Pages 11-16

  Sinclair, John ^a   Sim, Edith ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

acetyltransferase; arylamine; expression; GST fusion protein; NAT; purification

Indexed keywords

4 AMINOBENZOIC ACID; ACETYL COENZYME A; ARYLAMINE ACETYLTRANSFERASE; ARYLAMINE ACETYLTRANSFERASE 1; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; RADIOISOTOPE; UNCLASSIFIED DRUG;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME PURIFICATION; ENZYME SUBSTRATE; HUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION;

ACETYL COENZYME A; ACETYLATION; ARYLAMINE N-ACETYLTRANSFERASE; CLONING, MOLECULAR; GLUTATHIONE TRANSFERASE; HUMANS; PEPTIDE FRAGMENTS; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031060709     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(96)00592-8     Document Type: Article

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