Inhibition of Lon protease by bacterial lipopolisaccharide (LPS) though inhibition of ATPase

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Inhibition of Lon protease by bacterial lipopolisaccharide (LPS) though inhibition of ATPase

Lon protease, an ATP-dependent protease in Escherichia coli, degrades abnormal proteins and regulates several important cellular functions. Here we show novel inhibitory effects of lipopolysaccharide (LPS) on Lon protease activities. LPS inhibited the peptidase, protease, and ATPase activities of Lon; and a dose-response study showed that LPS at low doses more effectively inhibited the ATPase a...

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Actin-myosin subfragment-1 (SF-1) or actin-heavy meromyosin is dissociated by the binding of ADP and vanadate (Vi) under conditions such that ADP alone does not dissociate the complex. The association constant of the stable complex M.ADP.Vi, in which M indicates myosin [Goodno, C. C. (1979) Proc. Natl. Acad. Sci. USA 76, 2620-2624] with actin is smaller than the average association constant of ...

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Inhibition of myosin ATPase by vanadate ion.

Inhibition of the myosin ATPase by vanadate ion (Vi) has been studied in 90 mM NaCl/5 mM MgCl2/20 mM Tris-HCl, pH 8.5, at 25 degrees C. Although the onset of inhibition during the assay is slow and dependent upon Vi concentration (kapp approximately 0.3 M-1 s-1), the final level of inhibition approaches 100%, provided the Vi concentration is in slight excess over the concentration of ATPase sit...

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ژورنال

عنوان ژورنال: Advances in Bioscience and Biotechnology

سال: 2013

ISSN: 2156-8456,2156-8502

DOI: 10.4236/abb.2013.44077