Covalent binding of 4-hydroxy-2-nonenal to lactate dehydrogenase decreases nadh formation and metmyoglobin reducing activity

Journal of Agricultural and Food Chemistry

Volumn 62, Issue 9, 2014, Pages 2112-2117

  Ramanathan, Ranjith ^a   Mancini, Richard A ^a   Suman, Surendranath P ^b   Beach, Carol M ^b  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

beef color; LDH; lipid oxidation; mass spectrometry; metmyoglobin reduction; NADH dependent cytochrome b5 reductase

Indexed keywords

4-HYDROXY-2-NONENAL; CRITICAL COMPONENT; CYTOCHROME B5; LACTATE DEHYDROGENASE; LACTATE DEHYDROGENASE ACTIVITIES; LDH; LIPID OXIDATION; METMYOGLOBIN;

AMINO ACIDS; MASS SPECTROMETRY; SPECTROMETRY;

OXIDATION;

4 HYDROXYNONENAL; 4-HYDROXY-2-NONENAL; ALDEHYDE; LACTATE DEHYDROGENASE; METMYOGLOBIN; NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMISTRY; MASS SPECTROMETRY; MEAT; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PROTEIN BINDING; SKELETAL MUSCLE;

ALDEHYDES; AMINO ACID SEQUENCE; ANIMALS; CATTLE; L-LACTATE DEHYDROGENASE; MASS SPECTROMETRY; MEAT; METMYOGLOBIN; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; NAD; OXIDATION-REDUCTION; PROTEIN BINDING;

EID: 84897728813     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf404900y     Document Type: Article

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