Membrane reconstitution in CHL-R mutants of Escherichia coli K 12 V. ATPase incorporation into particles formed by complementation |
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Authors: | G Giordano C Riviere E Azoulay |
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Institution: | Laboratoire de Chimie Bacterérienne, C. N. R. S., 13274 Marseille Cedex 2 France |
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Abstract: | Mechanical treatments of cell suspensions of Escherichia coli K 12 strain PA 601, and its two mutants chl A− and chl B−, in a buffer without Mg2+ lead to partial solubilization of membrane-bound ATPase. After ultracentrifugation of cell-free extracts, ATPase can be recovered in the soluble fraction. Contrary to membrane ATPase, the soluble enzyme has the following properties: (1) it is insensitive to N,N′-dicyclohexylcarbodiimide; (2) heat-inactivation kinetics show a reactivation in the first 3 min and the half-time is 15 min; (3) ADP is a substrate. In the course of complementation between soluble fractions of mutants chl A− and chl B−, a part of soluble ATPase is incorporated into the newly formed particles. The specific activity of these particles is nearly the same as that of native particles; the ATPase bound to native membrane and the ATPase bound to the newly-formed particles both have the same biochemical properties. |
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Keywords: | KDO 2-keto-3-deoxyoctulosonate |
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