Results 141 to 150 of about 2,416 (164)

Characterization of a Bifunctional Cytidine 5′-Monophosphate N-acetylneuraminic acid Synthetase Cloned from Streptococcus Agalactiae

Biotechnology Letters, 2006
Recombinant CMP-sialic acid synthetase, cloned from Streptococcus agalactiae serotype V strain 2603 V/R, is bifunctional having both CMP-sialic acid synthetase and acetylhydrolase (acylesterase) activities. The enzyme is active over a wide pH range with an optimal CMP-sialic acid synthetase activity at pH 9.0 and an optimal acetylhydrolase activity at ...
Hui, Yu, Wesley, Ryan, Hai, Yu, Xi, Chen
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The functional expression of murine cytidine 5'-monophosphate N-acetylneuraminic acid transport protein in Escherichia coli

2021
The author retains copyright of this thesis. It must only be used for personal non-commercial research, education and study. It must not be used for any other purposes and may not be transmitted or shared with others without prior permission. For further terms on this licence: https://rightsstatements.org/page/InC-EDU/1.0/?language=en Contact ...
J. Tiralongo
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Identification, expression and tissue distribution of cytidine 5′-monophosphate N-acetylneuraminic acid synthetase activity in the rat

Glycoconjugate Journal, 1998
We report the postnatal developmental profiles of N-acetylneuraminic acid cytidylyltransferase (EC 2.7.7.43) (CMP-Neu5Ac synthetase) in different rat tissues. This enzyme, which catalyses the activation of NeuAc to CMP-Neu5Ac, was detected in brain, kidney, heart, spleen, liver, stomach, intestine, lung, thymus, prostate and urinary bladder but not in ...
B, Revilla-Nuin, A, Reglero, J C, Feo, L B, Rodriguez-Aparicio, M A, Ferrero   +4 more
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Production of cytidine 5′‐monophosphate N‐acetylneuraminic acid using recombinant Escherichia coli as a biocatalyst

Biotechnology and Bioengineering, 2002
AbstractAn Escherichia coli strain expressing three recombinant enzymes, i.e., cytidine 5′‐monophosphate (CMP) kinase, sialic acid aldolase and cytidine 5′‐monophosphate N‐acetylneuraminic acid (CMP‐NeuAc) synthetase, was utilized as a biocatalyst for the production of CMP‐NeuAc. Both recombinant E. coli extract and whole cells catalyzed the production
Sun-Gu, Lee, Jeong-Oh, Lee, Jung-Kyu, Yi, Byung-Gee, Kim   +3 more
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Regulation of biosynthesis ofN-glycolylneuraminic acid-containing glycoconjugates: characterization of factors required for NADH-dependent cytidine 5?monophosphate-N-acetylneuraminic acid hydroxylation

Glycoconjugate Journal, 1993
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 ...
T, Kawano, Y, Kozutsumi, H, Takematsu, T, Kawasaki, A, Suzuki   +4 more
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Cloning and overexpression of a cytidine 5′-monophosphate N-acetylneuraminic acid synthetase from Escherichia coli

Journal of Molecular Catalysis B: Enzymatic, 2000
The gene for cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuAc) synthetase (EC2.7.7.43) was amplified from the total DNA of Escherichia coli 44277 through a primer-directed polymerase chain reaction and cloned into pUC19 between the sites EcoRI and SalI.
Xia, Guoqing, Han, Xing, Ding, Huiping, Yang, Shoujun, Zhang, Shuzheng, Jin, Cheng   +5 more
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Investigation of the Kinetic Mechanism of Cytidine 5‘-Monophosphate N-Acetylneuraminic Acid Synthetase from Haemophilus ducreyi with New Insights on Rate-Limiting Steps from Product Inhibition Analysis

Biochemistry, 1999
The presence of sialic acid as a component of cell surface lipooligosaccharides or capsular polysaccharides has been shown to be correlated with the virulence of a number of Gram-negative mucosal pathogens, including several Haemophilus and Neisseria spp. As part of our efforts to evaluate the role of sialic acid in the pathobiology of these organisms,
N M, Samuels, B W, Gibson, S M, Miller
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Cytidine-5'-monophosphate-N-acetylneuraminic acid. Asialoglycoprotein sialic acid transferase activity in liver and serum of patients with juvenile hepatic cirrhosis and alpha-1-antitrypsin deficiency.

Biochimica et biophysica acta, 1976
The molecular basis for the accumulation of a substance which displays the immunological reactivity of alpha-1-antitrypsin within vesicles of liver parenchymal cells of individuals with hepatic cirrhosis and serum alpha-1-antitrypsin deficiency remains unclear.
M S, Kuhlenschmidt, S P, Peters, O D, Pinkard, R H, Glew, H, Sharp   +4 more
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ChemInform Abstract: STRUCTURAL MODIFICATION OF N‐ACETYLNEURAMINIC ACID. 3. SYNTHESIS OF 7‐EPI‐, 8‐EPI‐ AND 7,8‐BIS‐EPI‐N‐ACETYLNEURAMINIC ACID AND THEIR BEHAVIOR TOWARDS CYTIDINE MONOPHOSPHATE SIALIC ACID SYNTHETASE

Chemischer Informationsdienst, 1985
AbstractDer aus den Vorstufen (Ia), (Ib) erhältliche NonuIopyranosidonsäureester (Ic) liefert bei der Behandlung mit l0proz. Essigsäure und Ac2O/Py das 8‐epi‐ (IIa) und 7‐epi‐N‐Acetyl‐neuraminsäurederivat (IIb) [die Konfiguration von (IIa) wird durch chemische Korrelation mit (I) über die Stufen (IIIa)‐(IIIc) gesichert].
E. ZBIRAL, H. H. BRANDSTETTER
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ChemInform Abstract: Base‐ and Sugar‐Modified Cytidine Monophosphate N‐Acetylneuraminic Acid (CMP‐Neu5Ac) Analogues (I) and (II) — Synthesis and Studies with α(2—6)‐Sialyltransferase from Rat Liver.

ChemInform, 2001
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Gesche Dufner, Ralf Schwoerer, Bernd Mueller, Richard R. Schmidt   +3 more
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