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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 | ||
عنوان مقاله [English] | ||
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چکیده [English] | ||
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آمار تعداد مشاهده مقاله: 883 تعداد دریافت فایل اصل مقاله: 912 |