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Kinetics of the actomysin ATPase Four or six states?
Author(s) -
Leonard A. Stein
Publication year - 1991
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(91)80100-h
Subject(s) - state (computer science) , kinetics , statistical physics , chemistry , computational biology , econometrics , computer science , mathematical economics , biological system , mathematics , biology , physics , algorithm , classical mechanics
Tesi et al. [(1990) FEBS Lett. 260, 299/2‐232] use a misinterpretation of the four‐state controversy as a springboard to this paper. The authors give no data to characterize the proteins, making it impossible to compare the proteins with those from other laboratories. The analysis is flawed by the authors' failure to verify that the steady state rates obtained compared reasonably well with published rates. Although a four‐state model may be a satisfactory approximation for certain limited purposes, it is not a sufficient basis for a complete analysis of the actomyosin system.