Results 261 to 270 of about 480,870 (312)
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Analytical Biochemistry, 1981
Abstract Thiamine of high specific radioactivity has been prepared by catalytic incorporation of tritium using 3H2O and platinum. Purification of a crude commercially available product is described and the radiolabeling pattern is determined by NMR analysis of deuterated thiamine.
D R, Doerge, T, Sakurai, L L, Ingraham
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Abstract Thiamine of high specific radioactivity has been prepared by catalytic incorporation of tritium using 3H2O and platinum. Purification of a crude commercially available product is described and the radiolabeling pattern is determined by NMR analysis of deuterated thiamine.
D R, Doerge, T, Sakurai, L L, Ingraham
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Isotopic Labelling of Confined Carbyne
Angewandte Chemie, 2021AbstractCarbyne is a one‐dimensional allotrope of carbon consisting of a linear chain of carbon atoms bonded to each other with exceptional strength. Its outstanding mechanical, optical, and electronic properties have been theoretically predicted, but its stability has only been achieved when grown encapsulated in the hollow core of carbon nanotubes ...
Weili Cui +6 more
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Glutathione specifically labeled with isotopes
Analytical Biochemistry, 1985A procedure for synthesis of glutathione selectivity labeled with isotopes is described. A strain of Escherichia coli enriched in its content of gamma-glutamylcysteine synthetase and glutathione synthetase by recombinant DNA techniques is immobilized in a carrageenan matrix and treated with toluene to render the cells more permeable to the substrates ...
K, Murata +3 more
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Stable Isotopic Labeling for Proteomics
2011Since the coining of the term Proteome, the field of Proteomics has developed rapidly and come to rely heavily on mass spectrometry, initially for protein identification but recently the use of stable isotopic labels for protein quantitation has grown in importance.
Ashman, Keith +3 more
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2012
A great variety of technologies using stable isotope labeling in combination with mass spectrometry have been described being tools to identify and relatively quantify proteins within complex mixtures. Here, we present a method, termed isotope-coded protein label (ICPL), which is capable of high-throughput quantitative proteome profiling on a global ...
Kellermann, J., Lottspeich, F.
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A great variety of technologies using stable isotope labeling in combination with mass spectrometry have been described being tools to identify and relatively quantify proteins within complex mixtures. Here, we present a method, termed isotope-coded protein label (ICPL), which is capable of high-throughput quantitative proteome profiling on a global ...
Kellermann, J., Lottspeich, F.
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Labeling Monosaccharides With Stable Isotopes
2015Chemical and chemi-enzymic methods are discussed for the preparation of monosaccharide isotopomers that are singly and multiply labeled with (13)C, (2)H, (17/18)O, and (15)N isotopes. The discussion focuses primarily on chemical methods to incorporate stable isotopes into monosaccharides and not on methods to assemble labeled monosaccharides into more ...
Wenhui, Zhang +2 more
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LABELLING OF ANTIGENS BY VARIOUS ISOTOPES
Acta Endocrinologica, 1969ABSTRACT Isotopically labelled protein or polypeptide hormones are chemically and/or structurally different from the native material. This may be a major handicap when biological studies or radioimmunoassays are performed. Labelling procedures with 131I, 125I or by introduction of 3H (exchange, acetylation, alanylation) are described, and the ...
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Stable Isotope Labeling in Mammals (SILAM)
Cold Spring Harbor Protocols, 2008INTRODUCTIONA general approach in quantitative mass spectrometry is to mix a protein sample containing only natural-abundance isotopes with an identical protein sample containing proteins labeled with heavy stable isotopes (e.g., 2H, 13C, 15N, or 18O).
Daniel B, McClatchy, John R, Yates
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Isotope Labeling in Insect Cells
2012Target proteins in contemporary NMR are becoming increasingly complex. The interest lies on membrane proteins, multi-domain proteins, secreted proteins with secondary modifications etc., which can often only be expressed in eukaryotic expression hosts. Although E. coli is the organism of choice for expression of proteins in isotope labeled form for NMR
Alvar D, Gossert, Wolfgang, Jahnke
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ACS Chemical Neuroscience, 2020
Deuterium metabolic imaging (DMI) is a novel, 3D, magnetic resonance (MR)-based method to map metabolism of deuterated substrates in vivo. The replacement of protons with deuterons could potentially lead to kinetic isotope effects (KIEs) in which metabolic rates of deuterated substrates are reduced due to the presence of a heavier isotope. Knowledge of
Robin A. de Graaf +3 more
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Deuterium metabolic imaging (DMI) is a novel, 3D, magnetic resonance (MR)-based method to map metabolism of deuterated substrates in vivo. The replacement of protons with deuterons could potentially lead to kinetic isotope effects (KIEs) in which metabolic rates of deuterated substrates are reduced due to the presence of a heavier isotope. Knowledge of
Robin A. de Graaf +3 more
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