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  • 1985-1989  (3)
  • 1915-1919
  • Chemistry  (2)
  • Chemical Engineering  (1)
  • immune complexes  (1)
  • 1
    ISSN: 1573-2592
    Keywords: Anti-IgA antibodies ; IgA nephropathy ; immune complexes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The concentrations of serum IgG and IgM antibodies to polyclonal IgA (IgAp), IgA1, and IgA2 were determined by enzyme immunoassay in 31 patients with IgA nephropathy and 30 healthy controls. Patients with IgA nephropathy had significantly raised concentrations of serum IgA compared to controls (Mann-WhitneyU test,P=0.001) and increased concentrations of conglutinin-binding IgA immune complexes (P=0.024). No differences in the median concentrations of IgG and IgM anti-IgA antibodies were found between the patients and the controls. In serum samples from healthy controls there was a significant positive correlation between IgM anti-IgAp and IgA immune complex concentrations (P=0.05), which contrasted with the finding of an inverse correlation between IgM anti-IgAp and IgA immune complex concentrations in patients with IgA nephropathy (P〈0.05). In addition, the concentrations of conglutinin binding IgM immune complexes in serum were found to correlate with the concentration of IgM anti-IgAp (0.010〈P〈0.025), IgM anti-IgA1, and IgM anti-IgA2 (P«0.005 for both) in patients with IgA nephropathy but not in controls. IgM anti-IgA antibodies may be important in augmenting the clearance of IgA immune complexes from the serum of patients with IgA nephropathy.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 34 (1988), S. 293-304 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Experimental and theoretical studies on a backflush hollow-fiber enzymatic reactor (HFER) were conducted in this work for a lactose/lactase system. An A. niger lactase was chosen, from the four lactases tested, for reversible immobilization in the sponge layers of the fibers. An enzyme loading procedure was developed that allowed reliable and reproducible operation of the hollow-fiber reactor and produced industrially significant conversions without apparent change in the activity or stability of the lactase used. This reversible immobilization scheme also permitted easy replacement of the enzyme used. The performance of the backflush HFER was investigated and a large number of data concerning its operation were obtained and interpreted. Momentum and mass transports in such a HFER were analyzed, and mathematical models that took the experimental findings into consideration were also developed and solved analytically and/or numerically. Predictions from the computer model developed in this work were found to be in excellent agreement with the experimental data collected, suggesting the possibility of a priori design of a process-scale backflush HFER. With minor modifications, the models developed are expected to be applicable to hollow-fiber reactors with a wide selection of immobilized cells, organelles, and other enzymes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fast atom bombardment (FAB) and collisional activation dissociation (CAD) mass-analysed ion kinetic energy (MIKE) spectra have confirmed the structures of retinyl phosphate (Ret-P), retinyl phosphate mannose (Ret-P-Man) and guanosine 5′-diphospho-D-mannose (GDP-Man). Ret-P-Man was made in vitro while Ret-P and GDP-Man were chemically synthesized. Positive ion FAB mass spectrometry of Ret-P showed an observable short-lived spectrum with a mass ion at m/z 367 [M + H]+, and a major fragment ion at m/z 269 [M+H—H3PO4]+. Negative ion FAB mass spectrometry of Ret-P showed a strong stable spectrum with a parent ion at m/z 365 [M—H]-, a glycerol (G) adduct ion at m/z 457 [M—H+G]- and a dimer ion at m/z 731 [2M—H]-. GDP-Man showed an intense spectrum with parent ion at m/z 604 [M—H]- and cationized species at m/z 626 [M+Na-2H]- and 648 [M+2Na-3H]-. Negative ion FAB mass spectrometry of Ret-P-Man showed a parent ion at m/z 527 [M—H]- and a fragment ion at m/z 259 [C6H12PO9]-. The CAD-MIKE spectra showed structurally significant fragment ions at m/z 442 and 361 for the [M—H]- ion of GDP-Man, and at m/z 509, 406, 364 and 241 for the [M—H]- ion of Ret-P-Man. FAB and CAD-MIKE spectra have been applied successfully to confirm the structure of Ret-P-Man made in vitro from Ret-P and GDP-Man.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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