Metabolism of 4‐O‐Methyl‐N‐acetylneuraminic Acid a Synthetic Sialic Acid
Open Access
- 1 May 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 106 (2), 531-540
- https://doi.org/10.1111/j.1432-1033.1980.tb04600.x
Abstract
1 4-O-Methyl-N-acetylneuraminic acid shows a strong positive periodate-thiobarbiturate reaction. The mechanism of dye formation in this test for sialic acids is discussed in view of the studies already published. 2 An efficient preparation of a tritium-labelled 4-O-methyl-N-acetylneuraminic acid, with high specific radioactivity, by an oxymercuration-demercuration procedure is presented. 3 Sialyltransferase activities in microsomal fractions of equine liver using desialylated fetuin are studied. The enzyme activity, assayed in a radioactive procedure, shows an apparent Km value for CMP-N-acetylneuraminic acid of 0.7 mM, whereas this value is 3.4 mM for CMP-4-O-methyl-N-acetylneuraminic acid. Differences are also observed in the maximal velocity for the two substrates. 4 The equine liver system can be used to prepare substantial amounts of fetuin containing radioactive N-acetylneuraminic acid or 4-O-methyl-N-acetylneuraminic acid. The isolated reaction products show similar sialic acid release by treatments with acid or fowl-plague virus neuraminidase. In contrast, 4-O-methyl-N-acetylneuraminic acid-fetuin displays a marked resistance to desialylation by Vibrio cholerae neuraminidase. 5 Free 4-O-methyl-N-acetylneuraminic acid is completely resistant to the action of acylneuraminate pyruvate-lyase. It does not inhibit the enzymic cleavage reaction of N-acetylneuraminic acid. 6 The influence of a substitution at C-4 of neuraminic acid on the enzymatic reaction mechanisms is discussed.This publication has 44 references indexed in Scilit:
- Improved Synthesis of CMP-Sialates Using Enzymes from Frog Liver and Equine Submandibular GlandHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Carbon-13 nuclear magnetic resonance spin-lattice relaxation in the N-acylneuraminic acids. Probes for internal dynamics and conformational analysisJournal of the American Chemical Society, 1977
- Neuraminic acid-specific modification and tritium labelling of gangliosidesBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1977
- Substrate specificity of neuraminidasesJournal of Molecular Histology, 1973
- Activity of a Rat‐Liver Glycoprotein: Sialyltransferase Utilizing Desialyzed Prothrombin as an Acceptor in Normal and Hypothrombinemic AnimalsEuropean Journal of Biochemistry, 1973
- Inhibition of Acylneuraminate Pyruvate-Lyase: Evidence of Intermediary SCHIFF’s Base Formation and of a Possible Role of Histidine ResiduesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1971
- Studies on the Substrate Specificity of Acylneuraminate Pyruvate-LyaseHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1971
- Synthese von N-Acylneurammsäuren, II. N-[1-14C]Glykoloyl-, N-Chloracetyl- und N-FluoracetylneuraminsäureHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1970
- Differences in splitting capacity of virus and V. cholerae neuraminidases on sialic acid type substratesBiochemical and Biophysical Research Communications, 1967
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934