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- W1946194953 abstract "A sialyltransferase activity which catalyzes the synthesis of the trisialoganglioside GT1a from added disialoganglioside TD1a and CMP-N-acetylneuraminic acid has been demonstrated using a particulate fraction of 9-day-old embryonic chick brains. The enzyme exhibited optimum activity with the detergent Triton CF-54 and showed a broad pH optimum of 6.0 to 7.2. Ca2+ inhibited the reaction, whereas Mn2+, Mg2+, and EDTA had no effect. Slight elevations in activity were seen in the presence of Hg2+ or histone. The apparent Km for GD1a leading to GT1a was estimated to be 10(-3) M. When the monosialoganglioside, GM1, was used as the glycolipid substrate under conditions optimum for the synthesis of GR1a from GD1a, approximately 65% of the radioactive label was found in GD1a. However, about 50% of the remaining radioactivity was found in GT1a. The results suggest that the synthesis of GR1a could proceed via the sequence GM1 yields GD1a yields GT1a." @default.
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- W1946194953 date "1980-01-01" @default.
- W1946194953 modified "2023-10-16" @default.
- W1946194953 title "In vitro biosynthesis of an isomer of brain trisialoganglioside, GT1a." @default.
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- W1946194953 doi "https://doi.org/10.1016/s0021-9258(19)86219-1" @default.
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