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'Protein Phosphorylation' in keywords
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1990 (1)
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1Author    Hans Liidi, Bernhard Rauch, Wilhelm HasselbachRequires cookie*
 Title    The Influence of Detergents on the Ca2+-and Mg2+-Dependent Adenosine Triphosphatase of the Sarcoplasmic Reticulum  
 Abstract    During the stepwise solubilization of sarcoplasmic reticulum vesicles with detergents, the following changes in the structural and enzymatic properties of the preparation are observed: 1. The viscosity of the vesicular suspension initially rises. This change is accompanied by the formation of elongated tubules. Subsequently the membranes are completely desintegrated, resulting in a considerable reduction of the viscosity. 2. A decrease in the activity of the Ca2+-dependent ATPase, which is restored after complete solubilization. 3. A decrease in the change of intrinsic tryptophan-fluorescence on removal of calcium ions, which is also restored after complete solubilization. 4. A decrease of the calcium affinity of the ATPase. 5. A decrease in the amount of phosphorylated protein formed by the incorporation of inorganic phosphate. On the other hand, the amount of phosphoprotein formed from ATP is not affected during solubilization. 6. The dependence of the initial rates of phosphoprotein formation from inorganic phosphate on either magnesium or inorganic phosphate at low concentrations of the respective ligand changes from an S-shape profile to a normal hyperbolic profile after solubilization. 
  Reference    Z. Naturforsch. 37c, 299—307 (1982); received January 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum, ATPase, Detergent, Protein-Phosphorylation, Kinetics 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0299.pdf 
 Identifier    ZNC-1982-37c-0299 
 Volume    37 
2Author    Matthias Kuhn, Andreas Thiel, Peter BögerRequires cookie*
 Title    The 9-kDa Phosphoprotein Involved in Photoinhibition  
 Abstract    Photosystem-II particles exhibit strong photoinhibition. Short-term illumination of photosys-tem-II particles with high-intensity light (5000 piE/m 2 x s) leads to a typical change of the protein pattern on SDS-PAGE. Two proteins are mainly affected, namely the well-described 32-kDa herbicide-binding protein which probably is degraded [1] and, first published here, the 9-kDa phosphoprotein, whose function in the PS-II complex is still unknown. This protein is not de-graded, but seems to be linked to other polypeptides of the PS-II complex. During light treatment new bands of 23, 41, 50 and 54 kDa appear in the protein pattern of SDS-PAGE. A monospecific antiserum was produced against the 9-kDa phosphoprotein to investigate its fate. After light treatment the antibodies reacted with new proteins of higher molecular weights, most pronounced with a 23-kDa and a 41-kDa peptide. 
  Reference    Z. Naturforsch. 43c, 413—417 (1988); received February 15 1988 
  Published    1988 
  Keywords    9-kDa Phosphoprotein, Photosystem-II Particles, Photoinhibition, Protein Phosphorylation, Antibody 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0413.pdf 
 Identifier    ZNC-1988-43c-0413 
 Volume    43 
3Author    N. Pucheu, G.F W IldnerRequires cookie*
 Title    Isolation of 3 2 -3 5 kDa Thylakoid Proteins from Chlamydomonas reinhardii  
 Abstract    The protein com position o f Chlamydomonas reinhardii thylakoids in the m olecular weight range o f 3 2 -3 5 kDa was studied. The thylakoids were labelled with 32P —Pj in vivo using Pr starved cell cultures, solubilized with SDS and separated by polyacrylam ide gradient gel electrophoresis. The following differentiation o f proteins could be accom plished: two proteins were phosphorylated, which were also well stained with C oom assie blue, and one major protein was only detected by the silver staining procedure. The m obility o f the latter protein is different in gels with urea, showing an apparently lower molecular weight. In order to investigate whether a functional photosystem II is obligatory for protein phos­ phorylation, the phosphorylation o f thylakoid proteins was studied with a photosystem II deficient mutant. The mutant, which had normal photosystem I activity, but lacked photo­ system II activity, could synthesize ATP light dependently; its m ain labelled protein bands had a molecular weight o f 3 2 -3 5 kDa; it contained the light harvesting protein chlorophyll com plex and an unknown protein at 22 kDa. The 32P incorporation in photosystem II deficient cells was comparable to cells with functional photosystem II units. 
  Reference    Z. Naturforsch. 39c, 434 (1984); received N ovem ber 30 1983 
  Published    1984 
  Keywords    Photosystem II Complex, Q B-Protein, Chlamydomonas reinhardii, Protein Phosphorylation, Photosystem II Deficiency 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0434.pdf 
 Identifier    ZNC-1984-39c-0434 
 Volume    39 
4Author    Virginia Massheimer, LuisM. Fernandez, AnaR. De BolandRequires cookie*
 Title    Stimulation of Calmodulin Binding to Skeletal Muscle Membrane Proteins by 1,25-Dihydroxy-Vitamin D 3  
 Abstract    Previous work has shown that 1,25-dihydroxy-vitamin D 3 rapidly increases calmodulin lev­ els of skeletal muscle membranes without altering the muscle cell calmodulin content. There­ fore, the effects of the sterol on the binding of calmodulin to specific muscle membrane pro­ teins were investigated. Soleus muscles from vitamin D-deficient chicks were treated in vitro for short intervals (5-15 min) with physiological concentrations of 1,25-dihydroxy-vitamin D 3. Proteins of mitochondria and microsomes isolated by differential centrifugation were sep­ arated on sodium dodecyl sulfate polyacrylamide gels. Calmodulin-binding proteins were identified by a [125I]calmodulin gel overlay procedure followed by autoradiography. 1,25-Di-hydroxy-vitamin D 3 increased the binding of labelled calmodulin to a major, calcium-inde­ pendent, calmodulin-binding protein of 28 Kda localized in microsomes, and to minor calmo­ dulin-binding proteins of 78 and 130 Kda proteins localized in mitochondria. The binding of [125I]calmodulin to these proteins was abolished by flufenazine or excess non-radioactive cal­ modulin. 1,25-Dihydroxy-vitamin D 3 rapidly increased muscle tissue Ca uptake and cyclic AM P levels and stimulated the phosphorylation of several membrane proteins including those whose calmodulin-binding capacity potentiates. Analogously to the sterol, forskolin increased membrane calmodulin content, calmodulin binding to the 28 Kda microsomal protein and 45Ca uptake by soleus muscle preparations. Forskolin also induced a similar profile of changes in muscle membrane protein phosphorylation as the hormone. These results suggest that 1,25-dihydroxy-vitamin D 3 affects calmodulin distribution in muscle cells through cyclic AMP-de-pendent phosphorylation of membrane calmodulin-binding proteins. These changes may play a role in the stimulation of muscle Ca uptake by the sterol. 
  Reference    Z. Naturforsch. 45c, 663—670 (1990); received October 2/November 3 1989 
  Published    1990 
  Keywords    1, 25-Dihydroxy-Vitamin D 3, Skeletal Muscle, Muscle Membranes, Calmodulin Binding, Protein Phosphorylation 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0663.pdf 
 Identifier    ZNC-1990-45c-0663 
 Volume    45