¹ From the Department of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14850

Osmotic shock is a procedure in which Gram-negative bacteria are treated as follows. First they are suspended in 0.5 M sucrose containing ethylenediaminetetraacetate. After removal of the sucrose by centrifugation, the pellet of cells is rapidly dispersed in cold, very dilute, MgCl₂. This causes the selective release of a group of hydrolytic enzymes. In addition, there is selective release of certain binding proteins. So far, binding proteins for D-galactose, L-leucine, and inorganic sulfate have been discovered and purified. The binding proteins form a reversible complex with the substrate but catalyze no chemical change, and no enzymatic activities have been detected. Various lines of evidence suggest that the binding proteins may play a role in active transport: (a) osmotic shock causes a large drop in transport activity associated with the release of binding protein; (b) transport-negative mutants have been found which lack the corresponding binding protein; (c) the affinity constants for binding and transport are similar; and (d) repression of active transport of leucine was accompanied by loss of binding protein. The binding proteins and hydrolytic enzymes released by shock appear to be located in the cell envelope. Glucose 6-phosphate acts as an inducer for its own transport system when supplied exogenously, but not when generated endogenously from glucose.

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This article has been cited by other articles:

				H. M. Kalckar The Periplasmic Galactose Binding Protein of Escherichia coli Science, November 5, 1971; 174(4009): 557 - 565. [Abstract] [PDF]

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