The Effect of Thiol Compounds on the Glutamate Affinity of the Chloroplastic Glutamine Synthetase from Mustard Leaves

Abstract
The chloroplastic glutamine synthetase taken from mustard leaves shows a positive cooperative glutamate binding. The S0.5-value depends on the DTE concentration in the homogenization buffer. Normal glutamate satura­tion kinetics have been found with the root enzyme and the enzyme of etiolated cotyledons. These are not influ­enced by thiol compounds. The possible function of the allosteric behaviour of GS2 is discussed.

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