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  • 1
    Electronic Resource
    Electronic Resource
    Histochemical demonstration of carbonic anhydrase activity in mast cells (1965)
    Springer
    Cellular and molecular life sciences 21 (1965), S. 628-629 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Carboanhydraseaktivität in Mastzellen der Ratte wurde mittels Modifikation der Methode vonHäusler 4 demonstriert. Kapillarendothel, Basalzellen des Zungenepithels und Muskelgewebe reagierten ebenfalls positiv.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02144045
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  • 2
    Electronic Resource
    Electronic Resource
    Leucine aminopeptase in the spleen (1962)
    Springer
    Cellular and molecular life sciences 18 (1962), S. 364-365 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Leucinaminopeptidase wird histochemisch in der Milz von Mäusen und Ratten untersucht. Eine besonders ausgeprägte Reaktion zeigte sich in der Zentralarterienwandung und in den umgebenden Reticulumzellen der weissen Pulpa. Im Bereich der roten Pulpa verhalten sich nur die Inseln positiv, während eine extramedulläre Hämatopoese vorkommt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172252
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  • 3
    Electronic Resource
    Electronic Resource
    Matrix vesicles in chicken epiphyseal cartilage. Separation from lysosomes and the distribution of inorganic pyrophosphatase activity (1979)
    Springer
    Calcified tissue international 28 (1979), S. 65-72 
    Details
    ISSN: 1432-0827
    Keywords: Matrix vesicles ; Epiphyseal cartilage ; Gradient centrifugation ; Lysosomal enzymes ; Inorganic pyrophosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The extracellular matrix vesicles from epiphyseal cartilage of chickens were isolated by differential centrifugation. The matrix vesicles obtained showed considerable activity of lysosomal enzymes. This appears to have been due to lysosomal contamination because when we used a new density gradient medium (Percoll®), the lysosomal enzyme activities and the activity of alkaline phosphatase could be totally separated. Electron microscopy of the alkaline phosphatase-rich fraction showed matrix vesicle-like structures. Phosphatase activities of the cells and matrix vesicles were further studied by Sephadex G-200 gel filtration. Specific magnesium-activated inorganic pyrophosphatase, distinct from nonspecific alkaline phosphatase, could be demonstrated in the cellular fraction. No such separate activity could be demonstrated in the matrix vesicle fraction, and it is supposed that the pyrophosphatase activity in the matrix vesicles originates from the alkaline phosphatase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441219
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  • 4
    Electronic Resource
    Electronic Resource
    Arylsulphatase in growing bones of rat (1977)
    Springer
    Cellular and molecular life sciences 33 (1977), S. 1287-1288 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Soluble arylsulphatase purified from growing bones of rats was fractionated into 3 components with mol. wt of 32,000–36,000, and characteristics similar to arylsulphatase B of other tissues. Serum strongly inhibited the 2nd component, slightly activated the 3rd and had no effect on the 1st.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01920137
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of histological fixation on carbohydrate-rich tissue compounds and their periodate consumption (1969)
    Springer
    Histochemistry and cell biology 18 (1969), S. 87-96 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The recovery of the periodate-reactive material in the rat liver and human costal cartilage after fixation and decalcination was estimated, determing the periodate consumption rate of the sections. Carnoy solution gave the best recovery, about from 60 to 75 per cent in the case of the rat liver and about 87 to 97 per cent in the case of cartilage. Formaldehyde yielded somewhat lover recovery, and addition of 80 per cent ethanol to it did not significantly increase the preservation of the carbohydrates. Direct determination of the periodate consumption rate offers a simple and reliable method for estimation of the recovery of the periodate-reactive material in histological samples.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309905
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  • 6
    Electronic Resource
    Electronic Resource
    Electrophoretic and histochemical studies of carbonic anhydrase activity (1965)
    Springer
    Histochemistry and cell biology 5 (1965), S. 279-288 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A simple method for separation of carbonic anhydrase activity into components by electrophoresis on cellulose acetate strips is described. With this method, using barbiturate buffer systems at various pH values, two main components of CAH in rat erythrocytes, and the splitting of each of these into two minor components were revealed. Two components were also observed in the CAH activity in kidney and lens homogenates, and one component in brain homogenate. A modification of Häusler's histochemical method for CAH was adapted for visualization of the electrophoretically separated bands. This rendered the evalution of the results easier than with the quantitative measurements alone. The quantitative measurement of CAH activity in electrophoretic strips corresponded with the degree of staining by the histochemical method. This among other facts supports the view of the specificity of the histochemical method used. Some examples of the histochemical staining pattern of the CAH activity in rat tissues are given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285793
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  • 7
    Electronic Resource
    Electronic Resource
    Histochemical demonstration of carbonic anhydrase activity in the uterus (1966)
    Springer
    Histochemistry and cell biology 6 (1966), S. 164-167 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Positive histochemioal reaction for carbonic anhydrase (CAH) activity was observed in the glandular and lining epithelium of human and rat uteri. The CAH activity in the rat endometrium showed cyclic changes during the estrous cycle. Only one main component of CAH activity was revealed by electrophoresis, under conditions when the erythrocytes showed several isozymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00308188
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of carbonic anhydrase (1978)
    Springer
    Histochemistry and cell biology 58 (1978), S. 183-192 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rabbits were immunized using human erythroxyte carbonic anhydrase B (HCA B) purified. by the modified methods of Armstrong et al. (1966) and Bernstein and Schraer (1972). The globulin fraction was isolated by ammonium sulphate precipitation. The anti-HCA B globulin was specific, when judged using the double diffusion technique of Ouchterlony and immunoelectrophoresis. No cross reaction with human erythrocyte carbonic anhydrase C was found, but cross reactions with erythrocyte carbonic anhydrase from rat, mouse and guinea pig were observed. Fluorescein isothiocyanate conjugated goat anti-rabbit globulin was used for the localization of HCA B in tissue sections and erythrocytes on slides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495718
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  • 9
    Electronic Resource
    Electronic Resource
    Histochemical demonstration of carbonic anhydrase activity in the alimentary canal (1966)
    Springer
    Histochemistry and cell biology 6 (1966), S. 168-172 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Carbonic anhydrase (CAH) activity was histochemically demonstrated in various parts of the alimentary canal of rat and in the stomach of man using the method of Waldeyer and Häusler (1959). The most intense histochemical reaction was observed in the parietal cells of the rat stomach, and reactions of decreasing intensity in the epithelial cells of the colon, appendix, jejunoileum, duodenum and oesophagus in the order mentioned. An intense reaction was also observed in the parietal cells of the stomach of man and a weak activity in the pyloric glands. After electrophoresis on cellulose acetate film the CAH activity in human and rat stomach mucosa showed one band with the same migration rate as the fastest moving band of the erythrocyte CAH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00308189
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  • 10
    Electronic Resource
    Electronic Resource
    Carbohydrate-rich compounds in the colonic mucosa of man. III. A preliminary report of some biochemical characteristics of the carbohydrate-rich components in normal colonic mucosa (1971)
    Springer
    Journal of molecular histology 3 (1971), S. 101-106 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Preparations of human colonic epithelial cells were obtained virtually free from contamination by connective tissue. A trichloroacetic acid-soluble carbohydrate-rich fraction was prepared after defatting, proteolytic digestion and trichloroacetic acid precipitation of proteins by precipitating the polysaccharides with ethanol and potassium acetate. Four components of acid mucosubstances were revealed on electrophoresis, three of them showing the presence of sulphate radicals. The periodate consumption rate of the preparation was over four times greater after methanolytic desulphation, and confirms previous results concerning the blocking of periodate reactivity by acid radicals. The analysis of the sample showed the presence of 15% protein, 14% hexose, 9% sialic acid, 6% hexosamine, 3% fucose and 3% uronic acid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01003055
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