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Protein chemistry chromatography

Methods based on liquid chromatography-mass spectrometry (LC-MS) and universally accepted search algorithms permit reliable identifications of low levels of proteins at high sensitivity [6]. Even semispecialized protein chemistry labs can readily identify proteins at the level of a few picomoles (10 pmol of a 50-kDa protein is 500 ng). Specialized groups with access to the latest advances in HPLC and mass spectrometry routinely work with subpicomolar quantities. Chemical proteomics as discussed here requires the more advanced equipment. [Pg.347]

Jossang, P. (1992). Origins of chromatography. Nature, London 356, 100 Leggat Baily, J. (1962). Techniques in Protein Chemistry. Elsevier, Amsterdam. [Pg.188]

Davy, K.W., Morris, C J. (1976). Applications of gas-liquid chromatography in protein chemistry. Determination of C-terminal sequences on nanomolar amounts of proteins. J. Chromatogr., 116(2), 305-314. [Pg.175]

Halophilic enzymes are very unstable in low salt concentrations. Because some of the important fractionation methods in protein chemistry, such as electrophoresis or ion-exchange chromatography, cannot be applied at high salt concentrations, the available fractionation methods are rather limited. This basic difficulty is the main reason why the number of halophilic enzymes studied in pure form is very small. [Pg.5]

Fig. 23.—Affinity chromatography of immune serum produced by immunization of a rabbit with nonviable cells of S. faecalis. Inset is the agar diffusion of antibodies and lactosyl polysaccharide from the same organism. (Reprinted with permission from Journal of Protein Chemistry, Volume 6, J. H. Pazur, M. E. Tay, B. A. Pazur, and F. J. Miskiel, pp. 387-399, copyright 1987 Journal of Protein Chemistry.)... Fig. 23.—Affinity chromatography of immune serum produced by immunization of a rabbit with nonviable cells of S. faecalis. Inset is the agar diffusion of antibodies and lactosyl polysaccharide from the same organism. (Reprinted with permission from Journal of Protein Chemistry, Volume 6, J. H. Pazur, M. E. Tay, B. A. Pazur, and F. J. Miskiel, pp. 387-399, copyright 1987 Journal of Protein Chemistry.)...
D. B. Kassel,T. G. Consler, M. Shallaby, P. Sekhri, N. Gordon, and T. Nadler, Direct coupling of an automated 2-dimensional microcolumn affinity chromatography-capillary HPLC system with mass spectrometry for biomolecule analysis. Techniques in Protein Chemistry VI, Academic Press, New York, 1995, pp. 39-46. [Pg.570]

H7. Hearn, M. T. W., and Hancock, W. S, The role of ion-pair reversed phase HPLC in peptide and protein chemistry. In Biological/Biomedical Applications of Liquid Chromatography II (G. L. Hawk, ed.), pp. 243-271, Dekker, New York, 1979. [Pg.290]

Strosberg, A.D. (1986). Affinity Chromatography of Proteins. In A Darbre (ed). Practical Protein Chemistry - A Handbook, p. 165, John Wiley Sons Ltd. [Pg.211]

Modern techniques of high pressure liquid chromatography and isotacho-phoresis have not yet made much impact on the biochemistry of carbohydrates, but will soon do so. Nevertheless, some problems remain, especially with regard to the detection of sugars, where procedures at least comparable in sensitivity to the use of dansyl reagents in protein chemistry are badly needed. [Pg.8]

Synge, Richard Laurence Millington (p. 52, Plate 44). Born in 1914 in Liverpool, he studied Biochemistry at Cambridge, Int. Wool Seer. 1938, Biochemist at Wool Industries Research Association, Leeds 1941-1943, Staff Biochemist Lister Inst, of Preventive Medicine, London, until 1948, then Head of Dept, of Protein Chemistry, Riwett Research Inst. Bucksburn, Aberdeen (1948-67), Biochemist, Food Research Institute, Norwich, 1967-1976. Shared Nobel Prize for Chemistry with A.J.P. Martin, 1952 for invention of partition chromatography. [Pg.272]

Reversed-Phase Liquid Chromatography (RPLC) is an important tool in protein chemistry. Examination of sorption isotherms revealed that alcohohc buffers did not desorb proteins near physiological pH in RPLC systems, while buffers containing a poly(ethoxy alcohol) surfactant did not desorb protein at pH 2, but they did at pH 7 with concentrations of surfactant apparently well above the critical micellar concentration (cmc) [2]. It has been proposed that a necessary condition for the desorption of a protein from a surface is that the surface tension of the solvent falls between that of the protein and the surface [6]. This condition is fiilfilled for many proteins with surfactant solutions near conditions of physiological pH and ionic strength. Therefore, it was expected that separations of proteins could be thieved in these conditions. [Pg.345]

Thin-layer chromatography (TLC) and the more modem technique—high-performance thin-layer chromatography (HPTLC)— have numerous applications in proteins chemistry. These techniques are used for the quantitative determinations of peptides (nanograms), identification of peptides in partially hydrolyzed proteins, correlation of chromatographic properties for peptides and their constituent amino acids, as well as identification and characterization of proteins present in small quantities. [Pg.1728]

During the course of protein chemistry research looking for fluorescent compounds sensitive to the surrounding hydrophobicity, Weber designed l-dimethylaminonaphthalene-5-sulfonyl chloride (DNS-Cl) in 1952 [23]. DNS-Cl reacts with primary and secondary amino compounds (Figure 6.2) to form a fluorescent derivative with a yellow-green fluorescence [24]. DNS—amino acids can be separated by both normal-phase and reversed-phase liquid chromatography [25] and... [Pg.137]


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See also in sourсe #XX -- [ Pg.185 , Pg.187 ]




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