partial purification and properties of l-glutamine: d-fructose 6-p amidotransferase from human placenta
نویسندگان
چکیده
the first enzyme of the pathway for uridine diphosphate n-acetyl-d-glucosamine (udpag) biosynthesis i.e. l-glutamine: d-fructose 6-p amidotransferase (e.c. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on deae-sephadex a-50. the enzyme showed optimal activity in a broad range of ph from 5.8 to 7.8 in both phosphate and cacodylate buffers. its k m value for d-fructose 6-p was found to be 2.14 mm. the enzyme was inhibited up to 76% in the presence of 0.12mm udpag. a k value of 6.6 ?m was obtained for the feedback inhibition of this enzyme by udpag
منابع مشابه
PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA
The first enzyme of the pathway for uridine diphosphate N-acetyl-D-glucosamine (UDPAG) biosynthesis i.e. L-glutamine: D-fructose 6-P amidotransferase (E.C. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on DEAE-Sephadex A-50. The enzyme showed optimal activity in a broad range of pH from 5.8 to 7.8 in both phosphate and cacodylate ...
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عنوان ژورنال:
journal of sciences islamic republic of iranجلد ۳، شماره ۱، صفحات ۰-۰
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