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  • 1
    Digitale Medien
    Digitale Medien
    Characterization of Catecholamine-Storage Organelles in Transplantable Phaeochromocytoma and Adrenal Glands of Rats (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The properties of the catecholamine-storing organelles from transplantable rat phaeochromocytoma and rat adrenal glands were compared by density gradient centrifugation. It was shown that tumour granules are more heterogeneous and less dense than adrenal granules. Both granule preparations can take up catecholamines and nucleotides by a process driven by an electrochemical proton gradient. Dopamine β-hydroxylase and glycoprotein III were analysed by immunological techniques. Glycoprotein III was shown to be a specific component of chromaffin granules. Tumour tissue (average weight 700 mg) contains amounts of these antigens comparable to those in 210 adrenals. The biosynthesis of granules in the tumour apparently occurs at a low rate, making turnover studies difficult. The transplantable rat phaeochromocytoma is very useful for studies on the uptake properties and the immunological characteristics of rat catecholamine storage granules because one tumour provides an amount of material that could otherwise be obtained only from a large number of adrenal glands.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08675.x
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  • 2
    Digitale Medien
    Digitale Medien
    Immunological studies on the acidic chromogranins and on dopamine β hydroxylase (EC 1.14.2.1) of bovine chromaffin granules (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb12201.x
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  • 3
    Digitale Medien
    Digitale Medien
    IMMUNOLOGICAL STUDIES ON A MEMBRANE PROTEIN (CHROMOMEMBRIN B) OF CATECHOLAMINE-STORING VESICLES (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00068.x
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  • 4
    Digitale Medien
    Digitale Medien
    Uptake of Nucleotides and Catecholamines by Chromaffin Granules from Pig and Horse Adrenal Medulla (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 35 (1980), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The uptake of nucleotides and Catecholamines into chromaffin granules from adrenals of pigs and horses is similar to that previously seen in bovine chromaffin granules. The rate of [3H]ATP uptake at 2 mM-ATP concentration was 0.42 ± 0.06 and 0.15 ± 0.02 nmol/mg protein/min for pig and horse granules, respectively. The apparent Km's were 1.37 mM for pig granules, 0.89 mM for horse granules, and 1.2 mM for ox granules. The sensitivity of the uptake for nucleotides and catecholamine to specific inhibitors was found to be similar in granules from pig and ox, indicating that the same mechanisms of uptake are involved in both species.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb12516.x
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  • 5
    Digitale Medien
    Digitale Medien
    Dopamine β-Hydroxylase and Other Glycoproteins from the Soluble Content and the Membranes of Adrenal Chromaffin Granules: Isolation and Carbohydrate Analysis (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: Chromogranin A and two other proteins (A1 and A2) of the soluble proteins of bovine chromaffin granules were isolated by extraction from polyacrylamide gels after electrophoresis. The carbohydrate content of these proteins was 5%, with galactose, N-acetylgalactosamine, and sialic acid as the main sugars. Membranes of chromaffin granules were solubilized with sodium dodecyl sulphate (SDS) and three glycoproteins were isolated by sequential affinity chromatography on Concanavalin A (Con A) and wheat germ lectin (WGL) Sepharose columns. Two glycoproteins, designated GP II and III, were found to have a high carbohydrate content of about 30%. Mannose, galactose, N-acetylgalactosamine, and sialic acid were the main sugars. In addition membrane-bound dopamine β-hydroxylase was isolated by this procedure. No significant differences between the carbohydrate composition of the membrane-bound and the soluble enzyme were revealed. It was shown that all four subunits of dopamine β-hydroxylase possess carbohydrate chains with an affinity for Con A. The isolation methods established in this study will be useful for immunological studies on these glycoproteins.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08691.x
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  • 6
    Digitale Medien
    Digitale Medien
    The Proteins of Catecholamine-storing Organelles (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 15 (1982), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb03759.x
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  • 7
    Digitale Medien
    Digitale Medien
    Kinetic study of the hydration mechanism of vitamin B6 and related compounds (1970)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 92 (1970), S. 6134-6139 
    Details
    ISSN: 1520-5126
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/ja00724a006
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  • 8
    Digitale Medien
    Digitale Medien
    Isolation and Immunological Characterization of a Glycoprotein from Adrenal Chromaffin Granules (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 42 (1984), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: A glycoprotein (s-GP III) was isolated from the soluble lysate of chromaffin granules by chromatography with immunoaffinity and lectin columns. An identical protein (m-GP III) was shown to be present in the granule membranes. The apparent molecular weight of these glycoproteins as determined by the electrophoresis system of Laemmli (1970) was 43,000 under reducing conditions. In the absence of mercaptoethanol they aggregated to dimers. Antisera were raised against both the soluble and the membrane-bound forms of this glycoprotein. With these antisera GP III was further characterized: Immunoreplicas were obtained after two-dimensional electrophoresis of soluble and membrane-bound proteins of chromaffin granules. GP III was identified as a protein with a rather broad pI (4.6-5.3), indicating microhetero-geneity. As shown by subcellular fractionation, m-GP HI is specifically confined to chromaffin granules. GP III can therefore be used as a marker for the membranes of these organelles. The soluble form is secreted from adrenal medulla during stimulation with carbamylcholine chloride. An immunologically identical antigen was detected in adeno- and neurohypophysis. The physiological function of GP III is still unknown. It does not demonstrate any of the enzymatic activities so far known to occur in chromaffin granules.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12704.x
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  • 9
    Digitale Medien
    Digitale Medien
    Bovine adrenal medulla: Synthesis and secretion of radioactively labelled catecholamines and chromogranins (1971)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 271 (1971), S. 193-203 
    Details
    ISSN: 1432-1912
    Schlagwort(e): Adrenal Medulla ; Chromogranin ; Catecholamines ; Synthesis ; Secretion
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00998580
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  • 10
    Digitale Medien
    Digitale Medien
    Bovine adrenal medulla: Subcellular distribution of newly synthesised catecholamines, nucleotides and chromogranins (1972)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 273 (1972), S. 43-61 
    Details
    ISSN: 1432-1912
    Schlagwort(e): Adrenal Medulla ; Chromaffin Granules ; Synthesis ; Catecholamines ; Nucleotides ; Chromogranins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00508079
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