Nonspecific lipid transfer protein in the assay of a membrane-bound enzyme CMP-N-acetyl-neuraminate:lactosylceramide sialyltransferase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Endocrinology,Biochemistry
Reference54 articles.
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Cited by 9 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Dependence of rat liver CMP-N-acetylneuraminate:GM1sialyltransferase (SAT IV) activity on the ceramide composition of GM1ganglioside;FEBS Letters;1996-04-01
2. Relationship of membrane phospholipid composition, lactosylceramide molecular species, and the specificity of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase to the molecular species composition of GM3 ganglioside.;Journal of Lipid Research;1995-06
3. Effect of Golgi membrane phospholipid composition on the molecular species of GM3 gangliosides synthesized by rat liver sialyltransferase.;Journal of Lipid Research;1994-11
4. Preparation of defined molecular species of lactosylceramide by chemical deacylation and reacylation withN-succinimidyl fatty acid esters;Lipids;1994-10
5. Mechanism of GM3 ganglioside synthesis. Kinetic study of rat liver CMP-N-neuraminate:lactosylceramide alpha 2,3-sialyltransferase employing 19 molecular species of lactosylceramide.;Journal of Biological Chemistry;1994-05
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