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  • Analytical Chemistry and Spectroscopy  (3)
  • 1995-1999  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Analysis of linear oligogalacturonic acids by negative-ion electrospray ionization mass spectrometry (1995)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 9 (1995), S. 1572-1575 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Linear oligogalacturonic acids (1,4-linked α-D-galacturonic acid oligomers), obtained by partial acid hydrolysis of orange polygalacturonides, were studied by negative-ion electrospray ionization mass spectrometry, without prior sample derivatization. After preparative separation using high-resolution anion-exchange chromatography, some fractions enriched in uronic acids were desalted, transferred into a methanol+water solution adjusted to pH 10, and directly submitted to electrospray ionization mass spectrometry in the negative-ion recording mode. Clear molecular mass assignments of the oligomers, covering a degree of polymerization between 4 and 7, were obtained.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290091521
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  • 2
    Electronic Resource
    Electronic Resource
    A new method for the preparation of polymeric porous layer open tubular columns for GC applicationPresented at the 17th International Symposium on Capillary Chromatography and Electrophoresis, Wintergreen, Virginia, USA, May 1995. (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 7 (1995), S. 471-475 
    Details
    ISSN: 1040-7685
    Keywords: porous layer open tubular column ; polymeric porous layer capillary column ; in situ polymerization ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new method to prepare polymeric PLOT columns by using in situ polymerization technology is described. The method involves a straightforward in situ polymerization of the monomer. The polymer produced is directly coated on the metal tubing. This eliminates many of the steps needed in conventional polymeric PLOT column preparation. Our method is easy to operate and produces very reproducible columns, as shown previously (T. C. Shen, J. Chromatogr. Sci. 30, 239, 1992). The effects of solvents, tubing pretreatments, initiators and reaction temperatures in the preparation of PLOT columns are studied. Several columns have been developed to separate (1) highly polar compounds, such as water and ammonia or water and HCN, and (2) hydrocarbons and inert gases. A recent improvement has allowed us to produce bonded polymeric PLOT columns. These were studied, and the results are included also. © 1995 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mcs.1220070506
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  • 3
    Electronic Resource
    Electronic Resource
    Unfolding and aggregation-associated changes in the secondary structure of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride as monitored by FTIR (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biospectroscopy 3 (1997), S. 121-129 
    Details
    ISSN: 1075-4261
    Keywords: FTIR spectroscopy ; aggregated state ; folding and unfolding ; D-glyceraldehyde-3-phosphate dehydrogenase ; guanidine denaturation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Physics
    Notes: The secondary structure of native D-glyceraldehyde-3-phosphate dehydrogenase was compared with its partially folded intermediate and aggregated states obtained during guanidine hydrochloride (GdnHCl) denaturation using transmission Fourier transform infrared (FTIR) and micro-FTIR measurements. The changes in the secondary structures indicated a partially folded intermediate formed in 0.1M GdnHCl solution without visible aggregation. Increasing the GdnHCl concentration resulted in aggregation of the enzyme along with changes in the secondary structure. Although similar relative amounts of the secondary structure were found in the aggregated and native states of the enzyme, the temporal variation of the secondary structure revealed a difference in the β-sheet structure between the aggregated and native states, suggesting that the aggregation resulted from further unfolding of the enzyme. In addition, FTIR data suggest that such aggregates are most likely mediated by specific intermolecular interactions and that the predominant driving force involved in aggregation may be a hydrophobic interaction between exposed surfaces of partially folded intermediates. © 1997 John Wiley & Sons, Inc. Biospect 3: 121-129, 1997
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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