o-Diphenol: Oxygen oxidoreductase from leaves of sugar cane

James Coombs; Carl Baldry; Christopher Bucke; Stephen P. Long

doi:10.1016/0031-9422(74)80226-8

o-Diphenol: Oxygen oxidoreductase from leaves of sugar cane

James Coombs, Carl Baldry, Christopher Bucke, Stephen P. Long

Research output: Contribution to journal › Article › peer-review

Abstract

A non-particulate o-diphenol: O₂ oxidoreductase (phenolase) has been isolated from leaves of sugar cane. Gel filtration produced two fractions MW 32000 and 130000. The preferred substrate was chlorogenic acid. Other o-diphenols (caffeic acid, catechol, pyrogallol, dihydroxyphenylalanine) all of which were slowly oxidized when tested alone, increased the rates of O₂ consumption obtained with catalytic amounts of chlorogenic acid. Both enzyme fractions were inhibited by thiols; thioglycollate, which acted in a non-competitive manner, was most effective.

Original language	English (US)
Pages (from-to)	2703-2708
Number of pages	6
Journal	Phytochemistry
Volume	13
Issue number	12
DOIs	https://doi.org/10.1016/0031-9422(74)80226-8
State	Published - Dec 1974
Externally published	Yes

Keywords

Gramineae
MW determination, chlorogenic acid, substrate specificity, inhibition, thioglycollic acid.
Saccharum sp.
phenoloxidase
sugar cane

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Plant Science
Horticulture

Online availability

10.1016/0031-9422(74)80226-8

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title = "o-Diphenol: Oxygen oxidoreductase from leaves of sugar cane",

abstract = "A non-particulate o-diphenol: O2 oxidoreductase (phenolase) has been isolated from leaves of sugar cane. Gel filtration produced two fractions MW 32000 and 130000. The preferred substrate was chlorogenic acid. Other o-diphenols (caffeic acid, catechol, pyrogallol, dihydroxyphenylalanine) all of which were slowly oxidized when tested alone, increased the rates of O2 consumption obtained with catalytic amounts of chlorogenic acid. Both enzyme fractions were inhibited by thiols; thioglycollate, which acted in a non-competitive manner, was most effective.",

keywords = "Gramineae, MW determination, chlorogenic acid, substrate specificity, inhibition, thioglycollic acid., Saccharum sp., phenoloxidase, sugar cane",

author = "James Coombs and Carl Baldry and Christopher Bucke and Long, {Stephen P.}",

year = "1974",

month = dec,

doi = "10.1016/0031-9422(74)80226-8",

language = "English (US)",

volume = "13",

pages = "2703--2708",

journal = "Phytochemistry",

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T2 - Oxygen oxidoreductase from leaves of sugar cane

AU - Coombs, James

AU - Baldry, Carl

AU - Bucke, Christopher

AU - Long, Stephen P.

PY - 1974/12

Y1 - 1974/12

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AB - A non-particulate o-diphenol: O2 oxidoreductase (phenolase) has been isolated from leaves of sugar cane. Gel filtration produced two fractions MW 32000 and 130000. The preferred substrate was chlorogenic acid. Other o-diphenols (caffeic acid, catechol, pyrogallol, dihydroxyphenylalanine) all of which were slowly oxidized when tested alone, increased the rates of O2 consumption obtained with catalytic amounts of chlorogenic acid. Both enzyme fractions were inhibited by thiols; thioglycollate, which acted in a non-competitive manner, was most effective.

KW - Gramineae

KW - MW determination, chlorogenic acid, substrate specificity, inhibition, thioglycollic acid.

KW - Saccharum sp.

KW - phenoloxidase

KW - sugar cane

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o-Diphenol: Oxygen oxidoreductase from leaves of sugar cane

Abstract

Keywords

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