Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi*
Substrate specificity of α2↔3‐sialyltransferases in ganglioside biosynthesis of rat liver golgi*
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大鼠肝脏高尔基体神经节苷脂生物合成中α2↔3-唾液酸转移酶的底物特异性*
DOI:
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发表时间:
1991
期刊:
影响因子:
--
通讯作者:
K. Sandhoff
中科院分区:
文献类型:
--
作者:
H. Iber;G. Echten;K. Sandhoff
The acceptor specificities of four sialyltransferases (I, II, IV and V) involved in ganglioside biosynthesis were studied in Golgi vesicles derived from rat liver. The activities of these sialyltransferases were strongly detergent-dependent. Competition experiments with different detergent concentrations using LacCer (Galβ14Glcβ11 Cer), GM1a [Galβ13GalNAcβ14(NeuAcα23)Galβ14Glcβ11 Cer] and GD1b [Galβ13GalNAcβ14(NeuAcα28NeuAcα23)Galβ14Glcβ1 1 Cer] as substrates, and as mutual inhibitors for ganglioside sialyltransferase activity, suggested that sialyltransferase IV was able to catalyze the sialyltransfer in α23 linkage to the galactose residues of LacCer as well as of GM1a and GD1b. The other three sialyltransferases (I, II and V) seemed to be quite specific for their respective glycolipid acceptors, LacCer, GM3 and GM1b, GD1a and GT1b. Furthermore the kinetic data showed that sialyltransferase I was inactive at higher detergent concentrations (> 75 μg Triton CF-54); under these conditions, formation of GM3 and GD1a was catalyzed only by sialyltransferase IV. These results have been integrated into a model for ganglioside biosynthesis and its regulation.
DOI:
10.1016/0005-2760(80)90080-6
发表时间:
1980
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Eppler,CM;Morré,DJ;Keenan,TW
通讯作者:
Keenan,TW