Regulation of biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates: characterization of factors required for NADH-dependent cytidine 5'monophosphate-N-acetylneuraminic acid hydroxylation.
Glycoconj J
; 10(1): 109-15, 1993 Feb.
Article
en En
| MEDLINE
| ID: mdl-8358221
The hydroxylation of CMP-NeuAc has been demonstrated to be carried out by several factors including the soluble form of cytochrome b5. In the present study, mouse liver cytosol was subjected to ammonium sulfate fractionation and cellulose phosphate column chromatography for the separation of two other essential fractions participating in the hydroxylation. One of the fractions, which bound to a cellulose phosphate column, was able to reduce the soluble cytochrome b5, using NADH as an electron donor. The other fraction, which flowed through the column, was assumed to contain the terminal enzyme which accepts electrons from cytochrome b5, activates oxygen, and catalyses the hydroxylation of CMP-NeuAc. Assay conditions for the quantitative determination of the terminal enzyme were established, and the activity of the enzyme in several tissues of mouse and rat was measured. The level of the terminal enzyme activity is associated with the expression of N-glycolylneuraminic acid in these tissues, indicating that the expression of the terminal enzyme possibly regulates the overall velocity of CMP-NeuAc hydroxylation.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Glicoconjugados
/
Ácido N-Acetilneuramínico Citidina Monofosfato
/
NAD
/
Ácidos Neuramínicos
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Glycoconj J
Asunto de la revista:
BIOQUIMICA
/
METABOLISMO
Año:
1993
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Estados Unidos