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Purification and properties of a phenol oxidase derived from suspension cultures of Mucuna pruriens by Harm J. Wichers; Geert J. Peetsma; Theo M. Malingré; Hindrik J. Huizing is a Agricultural and Biological Sciences article available to read on EtoBox.

What is Purification and properties of a phenol oxidase derived from suspension cultures of Mucuna pruriens about?

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.

Who reads Purification and properties of a phenol oxidase derived from suspension cultures of Mucuna pruriens?

Author

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

Publisher

Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 0032-0935)

Published

1984

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)