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. (1371). PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA. , 3(1), -.
. "PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA". , 3, 1, 1371, -.
. (1371). 'PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA', , 3(1), pp. -.
. PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA. , 1371; 3(1): -.

PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA

Journal of Sciences, Islamic Republic of Iran
مقاله 2، دوره 3، شماره 1، شهریور 1992    اصل مقاله (490.2 K)
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
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