Reversible inactivation and dissociation of glutamine synthetase of Neurospora crassa by urea
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The effect of urea on the stability and the state of aggregation of glutamine synthetase is reported. Substrates and modulators of this enzyme exert a protective effect against urea-induced loss of activity. On partial inactivation by urea, the enzyme appears to consist of a dimeric species and an intermediate, partially unfolded form. Subsequent to the removal of urea, the presence of substrates and effectors is necessary to bring about a reversal of inactivation and a return of the enzyme lo the native or near-native state.
1976 ◽
Vol 29
(6)
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pp. 405
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1974 ◽
Vol 12
(2)
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pp. 231-244
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2021 ◽
Vol ahead-of-print
(ahead-of-print)
◽
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