J. Biol. Chem., Vol. 259, Issue 5, 2748-2753, 03, 1984
Glycerol oxidase, a novel copper hemoprotein from Aspergillus japonicus. Molecular and catalytic properties of the enzyme and its application to the analysis of serum triglycerides
T Uwajima, Y Shimizu and O Terada
Glycerol oxidase purified from Aspergillus japonicus AT 008 had Mr =
400,000 and contained 1 mol of protoheme IX and 2 g atoms of copper/mol of
enzyme protein. The absorption maxima of the oxidized form were found at
557, 530, 420, 280, and 238 nm, and those of the reduced form at 557 and
430 nm. Anaerobic addition of glycerol to the enzyme produced both a shift
of the Soret band from 420 to 410 nm and bleaching of the alpha and beta
bands at 557 and 530 nm. The ESR spectrum of glycerol oxidase showed three
major signals at g = 1.99, g = 2.00, and g = 2.02. The signals at g = 1.99
and g = 2.02 were diminished by the anaerobic addition of glycerol, and the
three signals completely disappeared after the addition of either
dithionite or diethyldithiocarbamate. Exposure of glycerol oxidase to a
borate buffer of pH 10.0 resulted in activation of the enzyme with
concomitant enhancement of the ESR signals at g = 1.99 and g = 2.02. Since
glycerol oxidase acts predominantly on glycerol, the enzyme can be employed
in a specific colorimetric assay for serum triglycerides in combination
with lipoprotein lipase.
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