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  • 1
    Electronic Resource
    Electronic Resource
    Cyclic GMP-Dependent Protein Kinase and Phosphorylation of the Endogenous Substrate Proteins in the Rabbit Superior Cervical Ganglion (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: When the homogenate of rabbit superior cervical ganglia (SCG) was incubated in the presence of [γ-32P]ATP and Mg2+, two specific proteins were strongly labeled. Their apparent molecular weights were 90,000 and 54,000, respectively. The phosphorylation of the latter was significantly stimulated by 10–50 nM cyclic GMP but to a lesser extent by cyclic AMP, whereas that of the former was not stimulated significantly by either of the cyclic nucleotides. The purified protein kinase inhibitor from rabbit skeletal muscle did not inhibit the phosphorylation. These results indicated that the observed phosphorylation of 54K protein was dependent on cyclic GMP but not on cyclic AMP. When intact SCG was incubated in the presence of 32Pi, phosphorylation of 90K protein was stimulated by cyclic GMP, dibutyryl cyclic GMP, and 8-bromo-cyclic GMP (10 μM), whereas phosphorylation of 54K protein was not significantly stimulated by any of these substances. The present demonstration of endogenous cyclic GMP-dependent protein kinase activity and its endogenous substrate proteins raises a possibility that the physiological actions of cyclic GMP in SCG are mediated by the phosphorylation of these proteins. Key Words: Superior cervical ganglion—Slow synaptic transmission—Cyclic GMP—Protein phosphorylation—G-kinase—Muscarinic actions. Takahashi S. Y. et al. Cyclic GMP-dependent protein kinase and phosphorylation of the endogenous substrate proteins in the rabbit superior cervical ganglion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb03100.x
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  • 2
    Electronic Resource
    Electronic Resource
    Further purification and characterization of trehalases from the American cockroach,Periplaneta americana (1985)
    Springer
    Journal of comparative physiology 155 (1985), S. 553-560 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A soluble trehalase was purified more than 200-fold from the male accessory gland of the American cockroach,Periplaneta americana, by CM-cellulose, hydrophobic chromatography, and Sephacryl S-200 gel filtration. The final preparation was homogeneous as judged by polyacryl-amide gel electrophoresis in the absence and presence of SDS, isoelectric focusing, and immuno-diffusion tests. The purified enzyme was maximally active at pH 5.2, and showed high specificity for trehalose with aK m of 0.98 mM. The isoelectric point was 4.7. The molecular weight of the enzyme (75,000) was determined by molecular sieve chromatography and SDS-polyacrylamide gel electrophoresis. The amino acid composition was determined and compared with those of trehalases purified from other sources. The trehalase could be stained for carbohydrate with the periodic acid-Schiff's reagent following SDS-polyacrylamide gel electrophoresis, indicating that it was a glycoprotein. Another soluble trehalase and two types of fat body trehalases could be highly purified by the method described. A comparison of the properties of trehalases from the accessory gland and the fat body showed some resemblance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00694444
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the guanosine 3′∶5′-monophosphate-dependent protein kinase from silkworm eggs and analysis of the endogenous protein substrates (1985)
    Springer
    Journal of comparative physiology 155 (1985), S. 693-701 
    Details
    ISSN: 1432-136X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In a previous paper, two types of cyclic nucleotide-dependent protein kinases, namely cGMP dependent “G-kinase” and cAMP dependent “A-kinase”, in silkworm eggs has been reported (Takahashi et al. 1975; Takahashi 1976). One of these, G-kinase, has now been purified 2400-fold by means of ammonium sulfate fractionation, chromatography on hydroxylapatite, DEAE cellulose, and gel filtration. Some of the properties of the enzyme are described. The enzyme is highly dependent on cGMP; it is strongly inhibited by GTP in a noncompetitive manner not only for ATP but also for cGMP. GTP was found to be highly inhibitory on G-kinases from various tissues of the silkworm, but did not inhibit the A-kinase. Incubation of the egg extract with [γ-32P]ATP and Mg2+ led to the formation of three major32P-labelled proteins, with molecular weights of 42.000, 70.000 and 180.000 as analyzed by SDS polyacrylamide gel electrophoresis. Two of them corresponded to the subunits of vitellin. The silkworm vitellin was effectively phosphorylated both by the highly purified G-kinase and by the A-kinase. It is concluded that the G-kinase is involved in the phosphorylation of vitellin in developing silkworm eggs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00694583
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