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Characterisation of the enzyme intermediates of the sarcoplasmic transport ATPase by the use of inhibitors

MPG-Autoren
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Boll,  Werner
Max Planck Institute for Medical Research, Max Planck Society;

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Makinose,  Madoka
Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://www.degruyter.com/downloadpdf/j/znc.1983.38.issue-3-4/znc-1983-3-420/znc-1983-3-420.xml
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https://doi.org/10.1515/znc-1983-3-420
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Zitation

Boll, W., & Makinose, M. (1983). Characterisation of the enzyme intermediates of the sarcoplasmic transport ATPase by the use of inhibitors. Zeitschrift für Naturforschung, C: Journal of Biosciences, 38(3-4), 282-289. doi:10.1515/znc-1983-3-420.


Zitierlink: https://hdl.handle.net/21.11116/0000-0003-6338-F
Zusammenfassung
1. Based on a detailed reaction scheme of the phosphorylation process of the sarcoplasmic transport ATPase the inhibition mechanisms of benzoctamine, DIO 9, AMP-PNP and of Ca2+-ions at relatively high concentrations (1 ~ 100 μᴍ) were determined.

2. The inhibition mechanisms were analyzed by measuring the γ-phosphate exchange between ATP and ADP and evaluated by applying conventional and an extended Dixon plot procedures.

3. The kinetic patterns of the inhibition were shown to be compatible with the assumed reaction scheme.

4. Each inhibitor combines with definite intermediates: Benzoctamine with the interm ediate species ~ P; DIO 9 with E and MgE and Ca2+ at relatively hign concentrations with E.

5. The central interm ediate blocked by benzoctamine can partially exist as -benzoctamine which is detected as phosphoprotein after acid denaturation