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THE PREPARATION AND PROPERTIES OF o ‐DIPHENOL: OXYGEN OXIDOREDUCTASE FROM POTATO TUBERS
Author(s) -
ABUKHARMA D. A.,
WOOLHOUSE H. W.
Publication year - 1966
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.1966.tb05971.x
Subject(s) - oxidoreductase , chemistry , enzyme , specific activity , biochemistry , affinity chromatography , oxygen , chlorogenic acid , electrophoresis , enzyme assay , potency , metal , chromatography , in vitro , organic chemistry
S ummary An o ‐diphenol: oxygen oxidoreductase (E.C. 1.10.3.1) has been purified from potato tubers. The enzyme shows a similar affinity for a range of substrates although the affinity is highest for chlorogenic acid, which occurs naturally in potato tubers. The affinity for oxygen is relatively low (K m = 2.23 × 10 −4 m). The pattern of activity over a range of pH values varied considerably with different substrates. Ultracentrifuge studies and agar gel electrophoresis suggest the preparation is relatively pure although throughout purification the preparation showed an increasing cresolase as well as o ‐diphenoloxidase activity. It is suggested that the cresolase activity is a normal component of the enzyme activity which may well be of importance in vivo . The high potency of a number of inhibitors including the copper‐specific 3:4 dichlorophenyl serine suggests that this metal is an integral part of the prosthetic group.