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 | |
| State | Published - Dec 1974 |
| Externally published | Yes |
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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
Cite this
o-Diphenol : Oxygen oxidoreductase from leaves of sugar cane. / Coombs, James; Baldry, Carl; Bucke, Christopher; Long, Stephen P.
In: Phytochemistry, Vol. 13, No. 12, 12.1974, p. 2703-2708.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - o-Diphenol
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
N2 - 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.
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
UR - http://www.scopus.com/inward/record.url?scp=49549154239&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49549154239&partnerID=8YFLogxK
U2 - 10.1016/0031-9422(74)80226-8
DO - 10.1016/0031-9422(74)80226-8
M3 - Article
AN - SCOPUS:49549154239
VL - 13
SP - 2703
EP - 2708
JO - Phytochemistry
JF - Phytochemistry
SN - 0031-9422
IS - 12
ER -