Protection of one of the two reactive thiol groups in F-actin by ATP and phalloidin.

@article{Blackholm1981ProtectionOO,
  title={Protection of one of the two reactive thiol groups in F-actin by ATP and phalloidin.},
  author={Heinz Blackholm and Heinz Faulstich},
  journal={Biochemical and biophysical research communications},
  year={1981},
  volume={103 1},
  pages={
          125-30
        }
}
  • H. BlackholmH. Faulstich
  • Published 16 November 1981
  • Biology, Chemistry
  • Biochemical and biophysical research communications

Nucleotide in monomeric actin regulates the reactivity of the thiol groups.

It was shown that the thiol-shielding activity and the protective capacity of a nucleotide are interrelated with its binding capability to monomeric actin.

Disulfide cross-linking of caldesmon to actin.

The effect of glutaraldehyde and phalloidin on the conformation of F-actin.

In the present study, it is shown that glutaraldehyde — and phalloidin — induced modifications of F-actin decrease the flexibility of thin filaments.

The detection of denervation-induced structural changes in actin by phalloidin.

It has been shown earlier, that actin from denervated muscles is not readily polymerized and does not actively combine with heavy meromyosin, so it was of interest to use phalloidin which binds specifically to F-actin affects these bonds to study changes in the actin structure occurring during denervation.

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The dissociation of the phalloidin-actin complex.

The dissociation of the toxin and the breakdown of the filaments together with a concomitant release of Ca and ADP are interdependent events.

Synthesis of a protein-reactive ATP analog and its application for the affinity labeling of rabbit-muscle actin.

The synthesis of a protein-reactive ATP analog, S-dinitrophenyl-6-mercaptopurine riboside 5′-triphosphate, started from isopropylidated 6-mer captureurine and could not be depolymerized by ATP solutions at low ionic strength.

The selective blocking of the polymerization reaction of striated muscle actin leading to a derivative suitable for crystallization. Modification of Tyr-53 by 5-diazonium-(1H)tetrazole.

The polymerization reaction of rabbit muscle actin was completely inhibited by reaction of one amino acid side chain per protein monomer with 5-diazonium-(1H)[14C]tetrazole. A tryptic peptide

Effect of cytochalasin B on formation and properties of muscle F-actin.