Metabolism of 4-O-Methyl-N-acetylneuraminic Acid a Synthetic Sialic Acid

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Sialic Acid (n-acetylneuraminic Acid) in Human Serum.

A simple spectrophotometric method is described for the sialic acids which utilizes the reaction with resorcinol and extraction with butyl acetate-n-butanol as a solvent. Normal values for adults, utilizing N-acetylneuraminic acid as a standard, were found to be 60 ± 10.4 mg./100 ml. Values for newborn babies averaged 40.4 ± 5.7. Similar values were found for specimens from 2-month-old infants ...

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Sialic acids (N,7-O-diacetylneuraminic acid and N-acetylneuraminic acid) in Escherichia coli. I. Isolation and identification.

DeWitt, Charles W. (The Upjohn Co., Kalamazoo, Mich.) and Janet A. Rowe. Sialic acids (N,7-O-diacetylneuraminic acid and N-acetylneuraminic acid) in Escherichia coli. I. Isolation and identification. J. Bacteriol. 82:838-848. 1961.-Two sialic acids, N-acetylneuraminic acid and N,7-O-diacetylneuraminic acid, were obtained in crude mixtures from whole cells of Escherichia coli and from its endoto...

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Structure-guided saturation mutagenesis of N-acetylneuraminic acid lyase for the synthesis of sialic acid mimetics.

Analogues of N-acetylneuraminic acid (sialic acid, NANA, Neu5Ac), including 6-dipropylcarboxamides, have been found to be selective and potent inhibitors of influenza sialidases. Sialic acid analogues are, however, difficult to synthesize by traditional chemical methods and the enzyme N-acetylneuraminic acid lyase (NAL) has previously been used for the synthesis of a number of analogues. The ac...

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Corrigendum: 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...

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Characterization 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: 1980

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1980.tb04600.x