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A particulate enzyme preparation from horseradish root tissue was shown to catalyze the transfer of 2-acetamido-2-deoxy-D-[14C1]glucose from uridine diphosphate 2-acetamido-2-deoxy-D-[14C1]glucose to an exogenous acceptor molecule derived from horseradish peroxidase. The acceptor was produced from purified peroxidase by the action of a mixture of glycoside hydrolases covalently bound to Sepharose. The membrane preparation containing the transferase was purified approximately 12-fold by aqueous two phase distribution and by discontinuous sucrose density gradient centrifugation. Hydrolysis of the reaction product yielded glucosamine as the only radio-labeled substance. Precipitation of the reaction product by antiserum against peroxidase showed that the label was incorporated into peroxidase. The transferase utilized the acceptor most efficiently when only 12% of the 2-acetamido-2-deoxy-D-glucose was removed from the acceptor. The acceptor lost no accepting capabilities when heated to 100 degrees C for 3 min prior to assay. Trypsin treatment caused a 14% decrease in label incorporated while pronase treatment caused a 93% decrease,
E D Sevier, and
L M Shannon
January 1960,
Texas reports on biology and medicine,
E D Sevier, and
L M Shannon
March 1973,
Biochimica et biophysica acta,
E D Sevier, and
L M Shannon
November 1958,
Nature,
E D Sevier, and
L M Shannon
October 1975,
Biochemical and biophysical research communications,
E D Sevier, and
L M Shannon
July 1968,
Plant physiology,
E D Sevier, and
L M Shannon
June 1966,
Journal of biochemistry,
E D Sevier, and
L M Shannon
May 1978,
The Journal of biological chemistry,
E D Sevier, and
L M Shannon
October 2008,
Analytical biochemistry,
E D Sevier, and
L M Shannon
January 2005,
Biochemistry. Biokhimiia,
E D Sevier, and
L M Shannon
February 1974,
FEBS letters,
