D-aspartyl residue in a peptide can be liberated and metabolized by pig kidney enzymes

Amino Acids

Volumn 10, Issue 2, 1996, Pages 187-196

  Kera, Y ^a   Funabashi, K ^a   Matsumoto, T ^a   Watanabe, T ^a   Nagasaki, H ^b   Yamada, R ^a  

^a NAGAOKA UNIVERSITY OF TECHNOLOGY   (Japan)

^b DOSHISHA WOMEN'S COLLEGE OF LIBERAL ARTS   (Japan)

Author keywords

Alanine aminotransferase; Amino acids; Aspartate aminotransferase; Conversion of D aspartate to L amino acids; D Aspartate oxidase; D Aspartyl residue in peptides; Hydrolysis of glycyl D aspartate; Metallo enzyme

Indexed keywords

ALANINE; ALANINE AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; CHELATING AGENT; CILASTATIN; ENZYME INHIBITOR; GLUTAMIC ACID; GLYCINE; KIDNEY ENZYME; METALLOPROTEINASE; OXALOACETIC ACID; OXIDOREDUCTASE; PYRUVIC ACID;

AMINO ACID METABOLISM; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DECARBOXYLATION; ENZYME ACTIVITY; ENZYME INHIBITION; HYDROLYSIS; KIDNEY CORTEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM; SWINE;

ANIMALIA; SUS SCROFA;

EID: 0029869621     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00806591     Document Type: Article

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