Purification and spectroscopic studies on catechol oxidase from lemon balm (Melissa officinalis)

Phytochemistry

Volumn 81, Issue , 2012, Pages 19-23

  Rompel, Annette ^a   Büldt Karentzopoulos, Klaudia ^b   Molitor, Christian ^a   Krebs, Bernt ^b  

^a UNIVERSITY OF VIENNA   (Austria)

^b UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

Catechol oxidase; Melissa officinalis; Metallo proteine; Oxygen binding; Polyphenol oxidase; Type 3 copper center; Tyrosinase

Indexed keywords

CATECHOL OXIDASE; COPPER; HYDROGEN PEROXIDE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; ISOELECTRIC POINT; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; MELISSA OFFICINALIS; MOLECULAR GENETICS; MOLECULAR WEIGHT; OXIDATION REDUCTION REACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CATECHOL OXIDASE; COPPER; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; HYDROGEN PEROXIDE; ISOELECTRIC POINT; MELISSA; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PLANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SUBSTRATE SPECIFICITY;

CITRUS LIMON; MELISSA OFFICINALIS;

EID: 84864771901     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2012.05.022     Document Type: Article

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