Purification and properties of α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD), key enzyme of niacin synthesis from tryptophan, from hog kidney

Journal of Nutritional Science and Vitaminology

Volumn 42, Issue 3, 1996, Pages 173-183

  Egashira, Yukari ^a   Kouhashi, Hanae ^a   Ohta, Takeo ^a   Sanada, Hiroo ^a  

^a CHIBA UNIVERSITY   (Japan)

Author keywords

Aminocarboxymuconate semialdehyde decarboxylase; Decarboxylase; Hog kidney; Niacin; Picolinic carboxylase; Tryptophan

Indexed keywords

AMINOCARBOXYMUCONATE SEMIALDEHYDE DECARBOXYLASE; AMINOCARBOXYMUCONATE-SEMIALDEHYDE DECARBOXYLASE; AMMONIUM SULFATE; CARBOXYLYASE; ENZYME INHIBITOR; NICOTINIC ACID; TRYPTOPHAN;

ANIMAL; ARTICLE; BIOSYNTHESIS; CHROMATOGRAPHY; CYTOSOL; DRUG ANTAGONISM; ENZYMOLOGY; ISOLATION AND PURIFICATION; KIDNEY; KINETICS; METABOLISM; MOLECULAR WEIGHT; PH; PRECIPITATION; SWINE;

AMMONIUM SULFATE; ANIMALS; CARBOXY-LYASES; CHROMATOGRAPHY; CYTOSOL; ENZYME INHIBITORS; FRACTIONAL PRECIPITATION; HYDROGEN-ION CONCENTRATION; KIDNEY; KINETICS; MOLECULAR WEIGHT; NIACIN; SWINE; TRYPTOPHAN;

EID: 0030155420     PISSN: 03014800     EISSN: 18817742     Source Type: Journal    
DOI: 10.3177/jnsv.42.173     Document Type: Article

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