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
. (1992). PARTIAL PURIFICATION AND PROPERTIES OF
L-GLUTAMINE: D-FRUCTOSE 6-P
AMIDOTRANSFERASE FROM HUMAN
PLACENTA. (e31198). Journal of Sciences, Islamic Republic of Iran, 3(1), e31198
MLA
. "PARTIAL PURIFICATION AND PROPERTIES OF
L-GLUTAMINE: D-FRUCTOSE 6-P
AMIDOTRANSFERASE FROM HUMAN
PLACENTA" .e31198 , Journal of Sciences, Islamic Republic of Iran, 3, 1, 1992, e31198.
HARVARD
. (1992). 'PARTIAL PURIFICATION AND PROPERTIES OF
L-GLUTAMINE: D-FRUCTOSE 6-P
AMIDOTRANSFERASE FROM HUMAN
PLACENTA', Journal of Sciences, Islamic Republic of Iran, 3(1), e31198.
CHICAGO
, "PARTIAL PURIFICATION AND PROPERTIES OF
L-GLUTAMINE: D-FRUCTOSE 6-P
AMIDOTRANSFERASE FROM HUMAN
PLACENTA," Journal of Sciences, Islamic Republic of Iran, 3 1 (1992): e31198,
VANCOUVER
. PARTIAL PURIFICATION AND PROPERTIES OF
L-GLUTAMINE: D-FRUCTOSE 6-P
AMIDOTRANSFERASE FROM HUMAN
PLACENTA. J. Sci. I. R. I.. 1992;3(1):e31198.
Journal of Sciences, Islamic Republic of Iran