## Abstract The pH dependence of previously reported effects of adenosine triphosphate (ATP) and ethylenediaminetetraacetate (EDTA) on cation binding by rat liver microsomes was studied by an equilibration and washing procedure. Equilibration of microsomes in media containing 95 mM NaCl and 4 mM Mg
The involvement of pH, Adenosine triphosphate, calcium, and magnesium in the contraction of the glycerinated stalks of Vorticella
โ Scribed by Townes, Mary M. ;Brown, Dugald E. S.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1965
- Tongue
- English
- Weight
- 648 KB
- Volume
- 65
- Category
- Article
- ISSN
- 0095-9898
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โฆ Synopsis
A glycerinated Vorticella stalk is prepared which remains relaxed at pH 6.8 or lower but contracts maximally when the pH is raised from 6.8 to 7.0. At pH 6.8, a maximum contraction is also produced when the Ca++ concentration is iacreased to 3 ,u M.
The degree of relaxation below pH 6.8 is fostered by ATP and Mg+ + which, along with C a + + , determine the degree of contraction at pH 7.0. A major role of calcium on the pH-induced contraction is to lower the pH-threshold from pH 7.5, obtaining in its absence to a stable value of pH 6.8. The only condition in which ATP is shown to cause a maximum contraction is at pH 7.0 in a medium containing 6 X M Mg++ and 3 X Ca++. It is considered that Ca++, Mg++, and ATP react with the contractile proteins to form a contractile complex which is in the relaxed form at pH 6.8. At this pH an increase of 0.2 pH units or the addition of shortened form, a contraction ensuing.
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