An enzymatically active truncated form (-55 N-terminal residues) of rabbit gastric lipase. Correlation between the enzymatic activity and disulfide bond oxydo-reduction state

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1386, Issue 1, 1998, Pages 39-49

  De Caro, Josiane ^a   Verger, Robert ^a   De Caro, Alain ^a  

^a Centre National de la Recherche Scientifique   (France)

Author keywords

Disulfide bridge; DsbA; Gastric lipase; Monoclonal antibody; Rabbit; Tryptic digestion

Indexed keywords

DISULFIDE; TRIACYLGLYCEROL LIPASE;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME STRUCTURE, FUNCTION AND VARIABILITY; IMMUNOBLOTTING; IMMUNOREACTIVITY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; STOMACH;

AMINO ACID SEQUENCE; ANIMALS; CYSTEINE; CYSTINE; DISULFIDES; DITHIOTHREITOL; LIPASE; LIPOLYSIS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; RABBITS; SEQUENCE ANALYSIS; STOMACH; SULFHYDRYL REAGENTS; TRYPSIN;

ORYCTOLAGUS CUNICULUS;

EID: 0032575265     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00058-2     Document Type: Article

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