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  • 1
    Electronic Resource
    Electronic Resource
    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
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08691.x
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  • 2
    Electronic Resource
    Electronic Resource
    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
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb12201.x
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  • 3
    Electronic Resource
    Electronic Resource
    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
    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
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00068.x
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  • 4
    Electronic Resource
    Electronic Resource
    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
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1980.tb12516.x
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  • 5
    Electronic Resource
    Electronic Resource
    The Proteins of Catecholamine-storing Organelles (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 15 (1982), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1982.tb03759.x
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  • 6
    Electronic Resource
    Electronic Resource
    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
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00724a006
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  • 7
    Electronic Resource
    Electronic Resource
    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
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08675.x
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  • 8
    Electronic Resource
    Electronic Resource
    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
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1984.tb12704.x
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  • 9
    Electronic Resource
    Electronic Resource
    Theg-factor of the 181 keV level of99Tc and hyperfine fields of Tc in Fe, Co, Ni (1971)
    Springer
    The European physical journal 243 (1971), S. 166-170 
    Details
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Theg-factor of the 181 keV-level of99Tc has been redetermined by the spin rotation method. Measurements with polycrystalline sources of Tc in Fe, Co, and Ni yielded values of the hyperfine fields at the Tc nucleus. $$\begin{gathered} g = + 1.310(25) \hfill \\ H_{hf} (Tc{\mathbf{ }}in{\mathbf{ }}Fe) = ( - )290(15)kOe \hfill \\ H_{hf} (Tc{\mathbf{ }}in{\mathbf{ }}Co) = ( - )170(5)kOe \hfill \\ H_{hf} (Tc{\mathbf{ }}in{\mathbf{ }}Ni) = - 47.8(1.5)kOe. \hfill \\ \end{gathered} $$
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01397861
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  • 10
    Electronic Resource
    Electronic Resource
    Goldanskii-karyagin effect at mössbauerE2-transitions (1974)
    Springer
    The European physical journal 267 (1974), S. 61-70 
    Details
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Investigations of anisotropic Debye-Waller factors have been carried out mainly using the M1-transitions of57Fe and119Sn. For this case the theory of the Goldanskii Karyagin effect is well established. Mössbauer studies of electric quadrupole interactions in hafnium and tungsten compounds made it necessary to extend the theory to the more complex case of E2-transitions. As the investigated compounds show a strong axial anisotropy of the electric field gradient, a similar behaviour has to be expected in principle for the tensor of the mean-square displacements, which determines the Debye-Waller factor immediately. A fitting procedure taking into account an axial asymmetric Debye Waller factor is worked out and applied to measurements performed with several complex hafnium and tungsten fluorine compounds. With NaWO2F3 the quadrupole interactions of182W,183W, and184W have been measured yieldingQ 5/2+(183W)/Q 2+(182W)=0-86(6) andQ 2+(184W)/Q 2+(182W)=0.955 (3).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01680363
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