The catechol oxidase of bean leaves (Phaseolus vulgaris)
Keyword(s):
Bean leaf catechol oxidase was studied with a new colorimetric assay system. The enzyme, though specific for o-diphenols, had a relatively low affinity for catechol. Borate, which complexes with catechol, inhibited the enzyme. Results obtained with DEAE chromatography and sucrose density gradient electrophoresis indicated that the enzyme consisted of a group of isozymes whose assay was independent of contaminating peroxidase. Both catechol oxidase and peroxidase increased during leaf expansion.
1971 ◽
Vol 38
(2)
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pp. 151-164
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1983 ◽
Vol 50
(04)
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pp. 848-851
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1986 ◽
Vol 21
(2)
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pp. 187-207
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2017 ◽