S-Mercuration of rat sorbitol dehydrogenase by methylmercury causes its aggregation and the release of the zinc ion from the active site

Archives of Toxicology

Volumn 86, Issue 11, 2012, Pages 1693-1702

  Kanda, Hironori ^a   Toyama, Takashi ^a   Shinohara Kanda, Azusa ^b   Iwamatsu, Akihiro ^b,c,d   Shinkai, Yasuhiro ^a   Kaji, Toshiyuki ^e   Kikushima, Makoto ^a   Kumagai, Yoshito ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b KIRIN BREWERY CO LTD   (Japan)

^c RIKEN Center for Integrative Medical Sciences   (Japan)

^d Protein Research Network Inc   (Japan)

^e TOKYO UNIVERSITY OF SCIENCE   (Japan)

Author keywords

Aggregation; Covalent modification; Cysteine; Methylmercury; Sorbitol dehydrogenase

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; IDITOL DEHYDROGENASE; METHYLMERCURY; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUCCINATE DEHYDROGENASE; ZINC ION;

AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; MERCURIALISM; MOLECULAR WEIGHT; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; RAT; SECRETION (PROCESS);

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CYSTEINE; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; L-IDITOL 2-DEHYDROGENASE; LIVER; METHYLMERCURY COMPOUNDS; MOLECULAR SEQUENCE DATA; MUTATION; NAD; PEPTIDE MAPPING; RATS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; ZINC;

RATTUS;

EID: 84871181842     PISSN: 03405761     EISSN: 14320738     Source Type: Journal    
DOI: 10.1007/s00204-012-0893-4     Document Type: Article

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