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The effect on actin ATPase of phalloidin and tetramethylrhodamine phalloidin
Author(s) -
Pinaev George,
Schutt Clarence E.,
Lindberg Uno
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00724-n
Subject(s) - phalloidin , actin , atpase , atp hydrolysis , polymerization , chemistry , biophysics , biochemistry , microbiology and biotechnology , biology , cytoskeleton , enzyme , cell , polymer , organic chemistry
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.