| Literature DB >> 14342496 |
P V SUBBARAO, N S JEGANNATHAN, C S VAIDYANATHAN.
Abstract
1. An enzyme solely localized in the nuclear fraction of rat liver was found to convert 3-hydroxyanthranilic acid into a red product that was isolated and crystallized from the reaction mixture. The product was identified as cinnabarinic acid (2-amino-3-oxo-3H-phenoxazine-1,9-dicarboxylic acid) by comparing its properties with synthetic cinnabarinic acid. 2. The enzyme had optimum pH at 7.2. Heavy-metal ions like Ag(+), Hg(2+), MoO(4) (2-), Fe(2+) and Cu(2+) were inhibitory; Mn(2+) activated the reaction to a considerable extent. 3. The reaction was inhibited by mercaptoethanol, GSH and cysteine, and activated by p-hydroxymercuribenzoate and sodium arsenite, which may suggest the involvement of disulphide groups in the reaction.Entities:
Keywords: ANTHRANILIC ACID; ARSENICALS; BENZOATES; CELL NUCLEUS; COPPER; CYSTEINE; ENZYME INHIBITORS; EXPERIMENTAL LAB STUDY; GLUTATHIONE; HOMOGENATES; IRON; LIVER CYTOLOGY; LIVER ENZYMOLOGY; LIVER FUNCTION; MERCURY; METABOLISM; MOLYBDENUM; OXAZINES; OXIDOREDUCTASES; PHARMACOLOGY; RATS; SILVER
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Year: 1965 PMID: 14342496 PMCID: PMC1206787 DOI: 10.1042/bj0950628
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857