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Purification and properties of a phenol oxidase derived from suspension cultures ofMucuna pruriens

✍ Scribed by Harm J. Wichers; Geert J. Peetsma; Theo M. Malingré; Hindrik J. Huizing

Publisher
Springer-Verlag
Year
1984
Tongue
English
Weight
697 KB
Volume
162
Category
Article
ISSN
0032-0935

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✦ Synopsis

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 90 000 + 5 000 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.

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