Lactosylceramide molecular species specificity of rat liver CMP-N-acetylneuraminate:lactosylceramide sialyltransferase.
Six naturally occurring and three synthetic molecular species of lactosylceramide (LacCer) were used to examine the molecular species specificity of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase in a Golgi-rich fraction of rat liver. The enzyme molecular species specificity wa...
Main Authors: | H Kadowaki, L A Symanski, K E Rys-Sikora, R S Koff |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
1989-11-01
|
Series: | Journal of Lipid Research |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520382250 |
Similar Items
-
Effect of membrane lipids on the lactosylceramide molecular species specificity of CMP-N-acetylneuraminate:lactosylceramide sialyltransferase
by: H Kadowaki, et al.
Published: (1993-06-01) -
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.
by: H. Kadowaki, et al.
Published: (1995-06-01) -
Nonspecific lipid transfer protein in the assay of a membrane-bound enzyme CMP-N-acetyl-neuraminate:lactosylceramide sialyltransferase.
by: H Kadowaki, et al.
Published: (1988-01-01) -
Effects of inducers of differentiation on protein kinase C and CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase activities of HL-60 leukemia cells.
by: X J Xia, et al.
Published: (1989-02-01) -
A new assay for determining ganglioside sialyltransferase activities lactosylceramide-2,3-sialyltransferase (SAT I) and monosialylganglioside-2,3-sialyltransferase (SAT IV).
by: Cynthia Q Sun, et al.
Published: (2014-01-01)