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Is a four‐state model sufficient to describe actomyosin ATPase?
Author(s) -
Tesi Chiara,
Barman Thomas,
Travers Franck
Publication year - 1990
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(90)80110-5
Subject(s) - actin , atpase , biophysics , chemistry , cleavage (geology) , biochemistry , biology , enzyme , paleontology , fracture (geology)
Four‐ [(1984), J. Biol. Chem. 259, 11908] and six‐ [(1985) Science 227, 999] state models have been proposed for actomyosin ATPase. A key experiment in deciding between these is whether or not there is a transient P i burst at high actin. In the first, the cleavage and release of products rates are similar and the P i burst is low; in the second, there are additional product complexes and the P i burst is large. We reinvestigated the problem by carrying out burst experiments under the conditions in [(1985) Science 227, 999]. Since we find that the P i burst at high actin is low, we conclude that the four‐state model is sufficient to describe actomyosin ATPase.