Allosteric behavior of platelet myosin

The allosteric properties of platelet actomyosin and myosin have been further studied. At pH 7.2, both exhibit sigmoid kinetics with at least two interacting ATP binding sites. At pH 8.9, the velocity versus substrate curve is shifted to the right and becomes more sigmoidal. In contrast, at pH 5.5,...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1977-01, Vol.178 (2), p.451-458
Hauptverfasser:	Malik, Mazhar N., Stracher, Alfred
Format:	Artikel
Sprache:	eng
Schlagworte:	Actomyosin - blood Adenosine Diphosphate - pharmacology Adenosine Triphosphatases - blood Adenosine Triphosphate - pharmacology Allosteric Site Animals Blood Platelets - metabolism Calcium - pharmacology Cattle Hydrogen-Ion Concentration Kinetics Myosins - blood Urea - pharmacology
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