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Modification of actins by phallotoxins
Die Naturwissenschaften, 1977Phallotoxins bind to filamentous actin (F-actin) from liver or rabbit muscle with Kdiss approximately 10(-8) M. By this combination the structure of F-actin is stabilized to such an extent that it will be resistant to the depolymerizing action of 0.6 M KI and of deoxyribonuclease I, to denaturation by heat (70 degrees C), and to local ruptures caused ...
T Wieland, Theodor Wieland
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A microassay for phallotoxins: Quantification of phallotoxins in Amanita species
Analytical Biochemistry, 1982Abstract The phallotoxin-mediated protection of bovine pancreatic deoxyribonuclease I from specific inhibition by rabbit muscle actin has been employed for the assay of phallotoxins. The use of this assay permits the quantification of as little as 6.3 ng of phalloidin.
J E, Mullersman, J F, Preston
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Protection of Actin from Heat Denaturation by Various Phallotoxins
Biological Chemistry, 1976Phallotoxins protect F-actin from heat denaturation at a temperature of 70 degrees C for 3 min. This has been shown by difference spectroscopy. G-actin is not protected from heat denaturation by phalloidin. Among the various phallopeptides investigated, 4 toxic ones showed the same protecting ability, whereas non-toxic seco-compounds has no effect. The
Heinz Faulstich, T Wieland, H Faulstich
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Influence of phallotoxins and metal ions on the rate of proteolysis of actin
Biochemistry, 1978The rate of proteolytic degradation of rabbit skeletal muscle actin by trypsin, alpha-chymotrypsin, and, mainly, subtilisin was followed by dual wavelength spectroscopy at 285 nm by reference at 320 nm. Phalloidin and phallacidin, two toxic bicyclic heptapeptides from the mushroom Amanita phalloides, protect F-actin against degradation by the ...
T Wieland, Theodor Wieland
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Fluorescent phallotoxins as probes for filamentous actin
Journal of Muscle Research and Cell Motility, 1988Phallotoxins have been conjugated to four different fluorescent labels: fluorescein, tetramethylrhodamine, nitrobenzoxadiazole and coumarine. Although endowed with different substrate affinities, they are all specific for polymeric actin. Useful advantage can and has been taken of the special characteristics of the fluorescent phallotoxin derivatives ...
Faulstich, H. +3 more
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A protein-binding assay for phallotoxins using muscle actin
Analytical Biochemistry, 1977Abstract The high affinity of phallotoxins to filamentous actin ( K D = 3.6 × 10 −8 m ) has been used to assay small amounts of phallotoxins. The limit of detection was as low as 160 ng of phallotoxins. This is 50 times lower than the limit of all other procedures known so far.
H Faulstich
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The binding of fluorescent phallotoxins to actin in myofibrils
Journal of Muscle Research and Cell Motility, 1993Fluorescence microscope observation of myofibrils incubated with rhodamine-phalloidin and coumarine-phallacidin showed an initial appearance of fluorescence bands at the Z-lines and near the middle of the sarcomeres indicating preferential binding of dye to actin subunits located at both actin filament ends. After long incubation times (1-3 h) however,
D, Szczesna, S S, Lehrer
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Phallotoxin and actin binding assay by fluorescence enhancement
Analytical Biochemistry, 1992The fluorescence of five fluorophores conjugated to phallotoxins was found to be specifically enhanced upon binding to F-actin in a polymerizing buffer. Rhodamine phalloidin had the greatest fluorescence enhancement of ninefold. The fluorescence titration of rhodamine phalloidin by actin was shown to be consistent with stoichiometric binding.
Z J, Huang +3 more
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