The effect on actin ATPase of phalloidin and tetramethylrhodamine phalloidin.
Actin polymerization has been studied in the absence of excess nucleotide. Using G-actin ATP monomers, it was shown that mechanical shearing stimulates ATP hydrolysis. The procedures used enabled the detection of differential effects of phalloidin and tetramethylrhodamine-phalloidin, on the P(i)-release step of the actin ATPase. It is concluded that tetramethylrhodamine, in contrast to phalloidin, accelerates P(i)-release from actin filaments.
Pinaev
G
G
Department of Cell Culture, Institute of Cytology Russian Academy of Sciences, St. Petersburg.
Schutt
C E
CE
Lindberg
U
U
D000199:Actins / Q000096:biosynthesis / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D000818:Animals; D005374:Filtration; D006868:Hydrolysis / Q000187:drug effects; D007700:Kinetics; D015636:Magnesium Chloride; D010590:Phalloidine / Q000494:pharmacology*; D010710:Phosphates / Q000378:metabolism; D011189:Potassium Chloride; D011817:Rabbits; D012235:Rhodamines / Q000494:pharmacology*
D000199:Actins; D010710:Phosphates; D012235:Rhodamines; D015636:Magnesium Chloride; D010590:Phalloidine; C005358:tetramethylrhodamine; D011189:Potassium Chloride; D000251:Adenosine Triphosphatases