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Partial purification and characterization of dihydrobenzophenanthridine oxidase fromEschscholtzia californicacell suspension cultures

✍ Scribed by H. M. Schumacher; M. H. Zenk


Book ID
104696572
Publisher
Springer
Year
1988
Tongue
English
Weight
312 KB
Volume
7
Category
Article
ISSN
0721-7714

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Purification and properties of a phenol
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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 s