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  • Biochemistry and Biotechnology  (3)
  • Aging  (1)
Document type
Keywords
Publisher
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomedical science 7 (2000), S. 466-474 
    ISSN: 1423-0127
    Keywords: Aging ; Free radical ; Superoxide anion ; SOD ; Catalase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Oxygen free radicals have been proposed to be involved in the process of aging. Superoxide dismutase (SOD) and catalase are important for antioxidative defense. In this study, profiles of SOD, catalase, and their mRNA levels were investigated in the frontal, parietal, temporal and occipital lobes, subcortex and cerebellum of male Wistar rats at ages 1–21 months. The total SOD and Mn SOD activities increased with age and exhibited higher levels at 6 and 12 months but decreased thereafter. Activity of catalase showed a similar trend and notably peaked at 12 months. The mRNA levels of Cu/Zn SOD, Mn SOD, and catalase remained constant in all areas tested (frontal, parietal, temporal and occipital lobes, and subcortex) except the cerebellum. Post-transcriptional regulation was involved in modulating the enzymes' activities during aging. Furthermore, the rate of mitochondrial generation of the superoxide anion $$(O_2^{\bar .} )$$ increased gradually with aging. Taken together, the results suggest that the increase of oxidative potential and the loss of proper antioxidant defense in the rats appear to be highly involved in the aging process of the brain.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Cationic anti-DNA antibodies ; Lupus nephritis ; Heparin ; Two-dimensional polyacrylamide gel electrophoresis ; Immunoblotting ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The relationship between chemical properties of anti-DNA antibodies (Abs) and lupus nephritis was investigated. The anti-DNA Abs in sera from systemic lupus erythematosus (SLE) patients were separated by two-dimensional electrophoresis (2-DE) and immunoblotting with goat anti-human IgG Abs. Highly cationic anti-DNA Abs were detected in deoxyribonuclease I (DNase I)-treated sera from patients with lupus nephritis (in 8 of 9 cases) but not in the sera from SLE patients without nephritis (in 0 of 9 cases), normal subjects, or patients with other renal diseases (in 0 of 7 cases). The mean titers of anti-dsDNA Abs in patients with lupus nephritis were not significantly different from those in SLE patients without nephritis. The highly cationic anti-DNA Abs in the sera disappeared after incubation with heparin-Sepharose. These results suggest that highly cationic anti-DNA Abs are specific for lupus nephritis and may be involved in development of lupus nephritis via the binding to glycosaminoglycans on the endothelial cell surface.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1506-1510 
    ISSN: 0173-0835
    Keywords: Anti-hapten antibodies ; Fluorescein isothiocyanate ; Two-dimensional affinity electrophoresis ; Carrier ; Epitopic suppression ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Effects of a carrier, bovine serum albumin (BSA) and a hapten array, fluorescein isothiocyanate-conjugated dextran (FITC-DEX), on the production of anti-FITC antibodies in BALB/c mice were analyzed by two-dimensional affinity electrophoresis (2-D AEP). The mice were immunized with FITC-BSA, followed by immunizations with FITC-BSA, saline, BSA, human serum albumin (HSA), fluorescein (Flu), and FITC-DEX. The heterogeneity and quantity of anti-FITC antibodies were increased markedly during the second and third immunization with FITC-BSA. However, the production of anti-FITC antibodies with low affinity to FITC was suppressed by the second and third immunization with the carrier protein of BSA. The suppression of anti-FITC antibodies by immunization with BSA may be due to the major histocompatibility complex (MHC)-mediated competition through antigen processing and the clonal expansion of BSA-specific B cells because similar suppression was induced by the immunization with HSA. The hapten array of FITC-DEX generally suppressed the production of anti-FITC antibodies; however, immunization with free hapten of Flu did not affect the production significantly. This may indicate that cross-linking of anti-FITC antibodies on the surface of specific B cells via the binding of hapten array is required for the suppression.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0173-0835
    Keywords: Fluorescein isothiocyanate ; Antibody ; IgG subclasses ; Somatic mutation ; Two-dimensional affinity electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The immune response to different doses of a hapten of fluorescein isothiocyanate (FITC) in BALB/c mice was analyzed by two-dimensional affinity electrophoresis (2-D AEP). The mice were immunized with different doses (0.5 μg, 5 μg, 50 μg, 500 μg and 2.5 mg) of FITC-conjugated bovine serum albumin (BSA). The antibodies to FITC bovine serum albumin (BSA) were separated into a large number of IgG spots due to differences in their isoelectric points (pI) and binding affinity to FITC ligand immobilized in the gel. The IgG spots. showing identical affinity to the ligand but different pI, have been considered as an IgG family. The affinity and quantity of IgG families changed with the increase in FITC-BSA dosage. With a low dose (5 μg) most of the families showed high affinity (Kd 〈 1 μM). When the dose was increased, not only high affinity antibodies but also intermediate (1 μM 〈 Kd 〈 50 μM) and low affinity (Kd 〉 50 μM) antibodies were produced. The increase of FITC-BSA up to 500 μg markedly increased the quantity of IgG spots showing a variety of affinity to FITC. However, 2.5 mg FITC-BSA did not increase the quantity and heterogeneity of IgG spots significantly. The changes in the heterogeneity and quantity of anti-FITC antibodies and the subclass switch were observed over the course of immunization. The heterogeneity and the quantity of IgGl, IgG2b and IgG3 antibodies increased markedly during the first and the second immunization, whereas an increase in the heterogeneity and the quantity of IgG2a antibody was observed in the third immunization. This suggests that the subclass switch to IgGl, IgG2b and IgG3 and the somatic mutation of IgG1, IgG2b and IgG3 occur during the first and the second immunization, but the subclass switch to IgG2 and the somatic mutation of IgG2a seem to occur later than that of the other IgG subclasses.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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