The effect of phallotoxins on the structure of F-actin in myosin-free ghost muscle fibres of rabbit.
Using polarized UV fluorescent microscopy it has been shown that phallotoxins (phalloidin-sulfone, phalloidin-sulfoxide-B, phalloidin-sulfoxide-A and dithio-phalloidin) cause an increase in tryptophan fluorescence anisotropy of F-actin myofilaments in myosin-free ghost muscle fibres of rabbit. The results obtained are considered to be evidence of conformational changes in F-actin, induced by phallotoxins. These changes are irreversible to a significant extent, which points to a high degree of actin binding to both toxic and nontoxic phallotoxins.
D000199:Actins / Q000378:metabolism*; D000546:Amanitins / Q000494:pharmacology*; D000818:Animals; D002118:Calcium / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005454:Fluorescence Polarization; D008856:Microscopy, Fluorescence; D009119:Muscle Contraction; D009132:Muscles / Q000032:analysis*; D009218:Myosins / Q000502:physiology*; D011817:Rabbits; D014364:Tryptophan
D000199:Actins; D000546:Amanitins; C018358:phallotoxin; D014364:Tryptophan; D009218:Myosins; D002118:Calcium