4,8-Anhydro-N-acetylneuraminic acid. Isolation from edible bird's nest and structure determination
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منابع مشابه
Improved automated determination of bound N-acetylneuraminic acid in serum.
The method in which thiobarbituric acid is used for sialic acid determination was adapted to a fully automated procedure, in which the chromogen need not be extracted with an organic solvent. The entire procedure, including hydrolysis, requires 35 mm and 25 l of serum for one analysis, but 30 samples can be analyzed per hour. The procedure, slightly modified, can be used to measure as little as...
متن کاملIsolation and characterization of a trisialoganglioside from mouse brain, containing 9-O-acetyl-N-acetylneuraminic acid.
A new ganglioside, containing an alkali-labile linkage, was extracted from mouse brain and purified. It represents 3.6% of total lipid-bound sialic acid in the tissue and was obtained in pure form with a yield of about 35%. It contains sphingosine, glucose, galactose, N-acetylgalactosamine and sialic acid in the molar ratio 1:1:2:1:4 and, upon exhaustive sialidase treatment gives the monosialog...
متن کاملSynthesis of N-acetylneuraminic acid and of CMP-N-acetylneuraminic acid in the rat liver cell.
Adult male rats, under starving and normal conditions, were injected intravenously with N-acetyl[3H]mannosamine and after various time intervals the specific radioactivities of free N-acetylneuraminic acid (NeuAc) and CMP-N-acetylneuraminic acid were determined in the liver. The specific radioactivity of free NeuAc was high even within 20s after injection; the maximum was reached between 7 and ...
متن کاملCorrigendum: Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis process
The original version of this article contained an error in testing the kinetic parameters of CgNal towards pyruvate, in which the concentration of ManNAc (50 mM) was not in excess. This error was corrected by re-running the assay in the presence of excessive ManNAc (180 mM). The corrected kinetic parameters of CgNal towards pyruvate are shown in Table 1. These changes do not change the conclusi...
متن کاملCharacterization of a novel N-acetylneuraminic acid lyase favoring N-acetylneuraminic acid synthesis
N-Acetylneuraminic acid lyase (NAL, E.C. number 4.1.3.3) is a Class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) from pyruvate and N-acetyl-D-mannosamine (ManNAc). Due to the equilibrium favoring Neu5Ac cleavage, the enzyme catalyzes the rate-limiting step of two biocatalytic reactions producing Neu5Ac in industry. We report the biochemical charact...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1987
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1987.tb10622.x