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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 83 (1961), S. 4089-4093 
    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
    s.l. : American Chemical Society
    Journal of the American Chemical Society 82 (1960), S. 2076-2076 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Rabbits were immunized with chromomembrin B, i.e. a membrane protein isolated from chromaffin granules of bovine adrenal medulla. When the rabbit sera were tested by immunodiffusion in the presence of various detergents, only negative results were obtained, whereas with complement fixation antibodies could be demonstrated. With this method the subcellular distribution of chromomembrin B in bovine adrenal medulla was determined. The results demonstrate that this protein is specifically localized in the membranes of chromaffin granules. In the mitochondrial and microsomal fractions it is present only in small amounts which are attributable to a contamination of these fractions with chromaffin granules. The subcellular distribution of chromomembrin R in bovine splenic nerves indicates that this antigen is also found in the membranes of noradrenalinestoring vesicles of sympathetic nerve. Chromomembrin B or a related antigen was detected in chromaffin grades isolated from pig and rat adrenal and in those isolated from a human phaeochromocytoma. It is also present in total membranes obtained from posterior and anterior hypophysis, but it is absent from membranes isolated from parotid gland, liver and adrenal cortex. This paper illustrates how a membrane protein which requires detergents for its solubilization can be characterized and measured by immunological methods.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of organic chemistry 27 (1962), S. 614-616 
    ISSN: 1520-6904
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 92 (1970), S. 6134-6139 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 83 (1961), S. 1921-1924 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Geophysical prospecting 10 (1962), S. 0 
    ISSN: 1365-2478
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences , Physics
    Notes: The method of Far Terrain Corrections is described which permits contouring of terrain effects for distant topography; near terrain effects must be computed separately.The method is only slightly less accurate than standard graphical techniques and saves computing time. It is most useful in medium size surveys involving 100 to 2,000 observation points where the application of electronic computers is uneconomic.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 271 (1971), S. 193-203 
    ISSN: 1432-1912
    Keywords: Adrenal Medulla ; Chromogranin ; Catecholamines ; Synthesis ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. 3H-leucine and3H-tyrosine were added to the perfusion medium of isolated bovine adrenal glands in order to study the synthesis and secretion of radioactively labelled catecholamines and proteins. 2. Various times after the injection of the labelled amino acids the soluble proteins of the microsomal fraction were isolated and subjected to polyacrylamide gel electrophoresis in three different buffer systems. The distribution of protein-bound radioactivity within the gels was determined. Most of the label was found to be confined to proteins which behaved like the specific soluble proteins of chromaffin granules, i.e. the chromogranins. 3. Stimulation of the adrenal gland with carbachol induced a release of catechol-amines, protein, and protein-bound radioactivity. In the absence of Ca2+ the secretion of all these components was abolished. The highest specific radioactivity of the proteins secreted upon stimulation was reached 4 h after the injection of the labelled precursors. The labelled proteins, secreted upon stimulation, could be identified as chromogranins. 4. Carbachol induced the release of highly labelled catecholamines after the injection of3H-tyrosine. The highest specific radioactivity of these catecholamines was already observed at the first stimulation with carbachol i.e. 30 min after3H-tyrosine. 5. These results demonstrate that in isolated bovine adrenal glands radioactively labelled chromogranins and catecholamines can be synthesised and can be secreted upon stimulation with carbachol.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 273 (1972), S. 43-61 
    ISSN: 1432-1912
    Keywords: Adrenal Medulla ; Chromaffin Granules ; Synthesis ; Catecholamines ; Nucleotides ; Chromogranins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. The subcellular distribution of newly synthesised catecholamines, nucleotides and proteins was investigated in bovine adrenal medulla. 3H-tyrosine, 3H-leucine and 32P-phosphate were used as radioactive precursors (“pulse label”). 2. Already 3 min after infusion of 3H-tyrosine the bulk of the labelled catecholamines was present in the “large granules” (mitochondria, lysosomes and chromaffin granules). In the fractions from the density gradient the distribution of the labelled and the total catecholamines was the same. Analogous results were obtained at longer time intervals. 3. 3 min after infusion of 32P-phosphate the labelled nucleotides present in the “large granules” were concentrated in the mitochondrial fraction. At longer time intervals after infusion of 32P-phosphate (45 min and 4h) chromaffin granules had accumulated a larger portion of the labelled nucleotides, mitochondria contained less. 4. After infusion of 45Ca2+, the isotope present in the large granules was found to be concentrated in the mitochondria and in chromaffin granules. 5. After infusion of 3H-leucine the soluble proteins of the adrenal medulla rapidly became labelled. 4 h after 3H-leucine newly synthesised proteins could be demonstrated in a particle which was present in the large granule fraction and which equilibrated in density gradients in a position corresponding to 1.6 M sucrose. This particle can be differentiated from mitochondria, microsomes, lysosomes and the bulk of the chromaffin granules. The labelled soluble proteins of this particle were identified as chromogranins. It seems likely that this particle represents a newly formed chromaffin granule which differs in its properties from the bulk of mature granules. The membrane proteins of this particle were not significantly labelled. 6. After infusion of 32P-phosphate the phospholipids of the adrenal medulla became labelled. The subcellular distribution of these phospholipids was similar to that of a microsomal marker enzyme, glucose-6-phosphatase. Lysoclecithin was not significantly labelled. 7. In the light of these results the subcellular events leading to the formation of complete chromaffin granules are discussed.
    Type of Medium: Electronic Resource
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