PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA
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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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Journal title
volume 3 issue 1
pages -
publication date 1992-06-01
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