期刊论文详细信息
FEBS Letters | |
Identity of GD1C, GT1a and GQ1b synthase in Golgi vesicles from rat liver | |
Sandhoff, Konrad1  Iber, Heinrich1  | |
[1] Institut für Organische Chemie und Biochemie der Universität Bonn, Gerhard-Domagk-Straße 1, D-5300 Bonn 1, FRG | |
关键词: Glycosphingolipid; Ganglioside; Biosynthesis; Sialyltransferase; Cer; ceramide (N-acylsphingosine); Gal; galactose; GalNAc; N-acetylgalactosamine; Glc; glucose; NeuAc; N-acetylneuraminic acid; UDP-Gal; uridine 5′-diphosphogalactose; UDP-GalNAc; uridine 5′-diphospho-N-acetylgalactosamine; CDP-choline; cytidine 5′-diphosphocholine; CMP-NeuAc; cytidine 5′-monophospho-N-acetylneuraminic acid; GlcCer; glucosylceramide; Glc1→1Cer; LacCer; Galβ1→4Glcβ1→1Cer; G; ganglioside; M; monosialo; D; disialo; T; trisialo; | |
DOI : 10.1016/0014-5793(89)81022-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Competition experiments using GM1b, GD1a and GT1b as substrates, and as mutual inhibitors for ganglioside sialyltransferase activity in preparations of Golgi vesicles derived form rat liver, suggested that sialyl transfer to these three respective compounds, leading to gangliosides GD1C , GT1a and GQ1b, respectively, is catalyzed by one enzyme. These results are incorporated into a model for ganglioside biosynthesis and its regulation.
【 授权许可】
Unknown
【 预 览 】
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