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1981 (1)
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1979 (1)
1Author    Wemer Jahn, Heinz Faulstich, Axel Deboben, Theodor WielandRequires cookie*
 Title    Formation of Actin Clusters in Rat Liver Parenchymal Cells on Phalloidin Poisoning as Visualized by a Fluorescent Phallotoxin  
 Abstract    By staining of cryo-sections o f rat liver with a fluorescent phallotoxin, the distribution of filamentous actin in liver cells could be demonstrated by fluorescence microscopy. While in untreated livers filamentous actin forms an almost continous layer at the cell periphery, the poisoning by phalloidin leads to the formation of actin clusters, preferentially located near the cell membrane. 
  Reference    Z. Naturforsch. 35c, 467 (1980); received December 28 1979/February 22 1980 
  Published    1980 
  Keywords    Fluorescent Phallotoxin, Actin, Rat Liver 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0467.pdf 
 Identifier    ZNC-1980-35c-0467 
 Volume    35 
2Author    Peter Dancker, Agnes KlicheRequires cookie*
 Title    Cytochalasin B-Induced ATPase Activity of Actin: Dependence on Monomer Concentration  
 Abstract    We simultaneously measured polymerization and ATPase activity of actin induced by cytochalasin B. It was found that under all conditions tested, ATPase activity was proportional to the concentration of actin which was unpolymerized. In addition, it was found that conditions increasing ATPase activity also increase the velocity o f polymerization. From this we conclude that CB-induced ATPase activity is a property o f the actin monomers and that the "readiness" of the monomers to hydrolyze ATP is correlated with an increased capacity o f the monomers to polymerize. 
  Reference    Z. Naturforsch. 36c, 1050—1055 (1981); received June 19 1981 
  Published    1981 
  Keywords    Actin, Actin Polymerization, Cytochalasin B 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-1050.pdf 
 Identifier    ZNC-1981-36c-1050 
 Volume    36 
3Author    P. Dancker, I. LowRequires cookie*
 Title    Complex Influence of Cytochalasin B on Actin Polymerization  
 Abstract    In the presence of very low concentrations (about 2 x 10~7 m) of cytochalasin B (CB) the time course of actin polymerization is much more sigmoidal when followed by viscosity measurements than when followed by light scattering measurements. This suggests that under these conditions actin polymers do not immediately reach their final length but only via short "bent" polymers which can be detected only by light scattering but not by viscosity measurements. At higher CB concentrations (about equimolar to those of actin) CB reduces the average degree of polymeriza­ tion and favors the nucleation step necessary for polymerization. 
  Reference    Z. Naturforsch. 34c, 555—557 (1979); received March 13 1979 
  Published    1979 
  Keywords    Actin, Cytochalasin B, Cell Motility, Muscle Proteins, Micro filaments 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0555.pdf 
 Identifier    ZNC-1979-34c-0555 
 Volume    34