Purification and properties of a phenol oxidase derived from suspension cultures of Mucuna pruriens |
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Authors: | Harm J. Wichers Geert J. Peetsma Theo M. Malingré Hindrik J. Huizing |
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Affiliation: | (1) Laboratory of Pharmacognosy, State University of Groningen, Antonius Deusinglaan 2, NL-9713 AW Groningen, The Netherlands |
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Abstract: | From cells of Mucuna pruriens, grown in suspension, a monophenol monooxygenase (EC 1.14.18.1) was purified to homogeneity, as deduced from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme appeared to have a native molecular weight of 90000±5000 dalton, and consisted of two subunits, each of 42000±1000 dalton. High-performance liquid chromatography with electrochemical detection for specific measurement of catecholes, was used to determine separately the tyrosinehydroxylating and catecholase activities of the enzyme. For the enzymatic activities, pH optima of, respectively, 7.5 and 5.5–6.5 were found; the effects of some inhibitors on both activities appeared to be different. Michaelis-Menten characteristics for some mono-and o-dihydroxysubstrates were determined.Abbreviations DEAE diethylaminoethyl - HPLC high-performance liquid chromatography - L-DOPA L-3,4-dihydroxyphenylalanine |
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Keywords: | Cell culture (phenol oxidase) font-variant:small-caps" >L-3,4-Dihydroxyphenylalanine Mucuna (suspension culture, enzyme) Phenol oxidase Tyrosinase |
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