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  • 1975-1979  (5)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 97 (1975), S. 4261-4264 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 256 (1978), S. 391-391 
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 60 (1979), S. 155-168 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In relation to our earlier finding that the thyroglobulin-like material responsible for the cytochemical immunoreaction of C cells was obtained in the peak I fraction of Bio-Gel A-5 m, which included faster sedimenting components of thyroglobulin, the present study has identified the positive reacting component and clarified its immunochemical and immunohistochemical properties. 1. The peak I fraction of dog and hog thyroglobulin was chromatographed on a Bio-Gel A-50 m column. Antiserum to the faster eluted peak I 1 ′ only immunoreacted with C cells. The peak I 1 ′ was then refiltered on Bio-Gel A-150 m column. Antiserum to peak I 1 ″ fraction of both species which was eluted in the first part had high immune specificity for C cells. 2. When 4–30% and 2–16% continuous gradient gels of polyacrylamide were employed, peak I 1 ″ represented a single electrophoretic band corresponding to the component with the largest molecular weight in thyroglobulin. The protein was named C-thyroglobulin. The molecular weight was approximately 2,600,000, four times as large as 19 S, as calculated by relative mobility on the 2–16% gradient gel. 3. In double diffusion tests, anti-peak I 1 ″ antiserum produced two immunoprecipitin lines with its own antigen. The reaction was different from that of anti-19 S antiserum which formed a single line. 4. On immunoperoxidase staining, anti-peak I 1 ″ antiserum reacted to C cells in exactly the same way as anti-calcitonin antiserum. 5. When anti-peak I 1 ″ antiserum was absorbed with calcitonin, the subsequent reaction of the C cells was greatly decreased. The absorption of anticalcitonin antiserum with increased amounts of peak I 1 ″ abolished the C cell reaction. On the basis of these observations, the possibility that C-thyroglobulin is a biosynthetic precursor of calcitonin exists.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 33 (1977), S. 538-540 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary When the canine thyroid gland was stained by immunofluorescence and immunoperoxidase methods using undiluted thyroglobulin antiserum, a considerably stronger immunoreactivity was revealed in the parafollicular cells than in the colloid droplets and follicular cells. After induced hypercalcemia and antithyroid drug treatment, the immunoreactivity of the parafollicular cells coinciding with the movement of secretory granules containing calcitonin was conspicuously decreased. An application of diluted serum (above 1:10) produced a strong reaction in the colloid.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 187 (1978), S. 429-438 
    ISSN: 1432-0878
    Keywords: Parafollicular cells ; Thyroglobulin ; Larger molecular component ; Cross-reactivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Thyroglobulin-like immunoreactivity of the parafollicular cells was studied by an immunoperoxidase bridge technique using antisera against dog thyroglobulin fragments. 1. The dog parafollicular cells were specifically stained by anti-peak I (27S and larger components fraction) antiserum absorbed with peak II (19S fraction). By this method, they were easily distinguishable from the non-reactive follicular cells and colloid droplets. More sensitive staining of the parafollicular cells was possible with anti-peak I (larger components fraction) antiserum. The staining reactions indicated that the antigenic material responsible for immunoreactivity of the parafollicular cells was due to larger molecular components of thyroglobulin corresponding to 32S, 37S or 〉37S, and was not due to either the 19S thyroglobulin or to the 27S iodoprotein. 2. A conspicuous decrease of the immunoreactive material in the parafollicular cells occurred in the dog after both chronically induced hypercalcemia and antithyroid drug treatment. This coincided with movement of secretory granules containing calcitonin as shown by staining with silver impregnation, HCl-basic dye, and lead-hematoxylin. 3. The antisera against larger molecular components of dog thyroglobulin showed a high degree of cross-reactivity to the parafollicular cells of most of the mammalian species investigated; rats, rabbits, hamsters, mice, cats, lions, goats, cows, and human.
    Type of Medium: Electronic Resource
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