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'1' in keywords Facet   Publication Year 1990  [X]
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1990[X]
1Author    Gabriele Knörzer, Herm Ann Seyffer, W. Alter, SiebertRequires cookie*
 Title    Synthese von Diboraheterocyclen mit einer BC3B-Gruppierung Synthesis of Diboraheterocycles with a BC3B Unit  
  Reference    Z. Naturforsch. 45b, 1136—1138 (1990); eingegangen am 31. Januar 1990 
  Published    1990 
  Keywords    1, 3-Diborylpropanes, 1, 2-Diborolane, 1, 2, 6-Thiadiborinane, 1, 2, 6-Azadiborinane 
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 TEI-XML for    default:Reihe_B/45/ZNB-1990-45b-1136.pdf 
 Identifier    ZNB-1990-45b-1136 
 Volume    45 
2Author    M. Arianne Bäudler, JosefH. AhnRequires cookie*
 Title    Zur Existenz eines Triphosphacyclobutenid-Ions P3CH20 Contributions to the Chemistry of Phosphorus, 204 [1] On the Existence of a Triphosphacyclobutenide Ion P3C H 2e  
 Abstract    The structure o f the reaction product o f white phosphorus and sodium in diglyme which exhibits a low field AB2 system in the 31P {'H } N M R spectrum [4] has been reexamined. A c­ cording to the results o f a complete analysis o f its proton coupled 31P N M R spectrum (ABB'XX' system), the compound is the hitherto unknown 1,2,3-triphosphacyclopentadienide 
  Reference    Z. Naturforsch. 45b, 1139—1142 (1990); eingegangen am 9. Februar 1990 
  Published    1990 
  Keywords    Triphosphacyclobutenide Ion, 1, 2, 3-Triphosphacyclopentadienide Ion, Tetraphosphacyclopentadienide Ion, Phosphorus Heterocycles 
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 TEI-XML for    default:Reihe_B/45/ZNB-1990-45b-1139.pdf 
 Identifier    ZNB-1990-45b-1139 
 Volume    45 
3Author    Z. NaturforschRequires cookie*
 Title    Filippo Imperato  
 Abstract    A new pentaoxigenated xanthone has been iso­ lated from aerial parts o f the fern Cystopteris fra­ gilis. By spectroscopic and chemical methods this compound has been shown to be 1,6-dihydroxy-3,5,7-trimethoxyxanthone which is o f biosynthetic interest in ferns. 
  Reference    Z. Naturforsch. 45b, 1603—1604 (1990); received June 1 1990 
  Published    1990 
  Keywords    Cystopteris fragilis, Pteridophyta, Aspleniaceae, 1, 6-Dihydroxy-3, 5, 7-trimethoxyxanthone 
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 TEI-XML for    default:Reihe_B/45/ZNB-1990-45b-1603_n.pdf 
 Identifier    ZNB-1990-45b-1603_n 
 Volume    45 
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