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- W1966287972 abstract "Abstract The NADP+ specific glutamate dehydrogenase from wild-type Neurospora crassa forms a stable binary complex with NADPH. This can combine with L-glutamate, α-ketoglutarate or the substrate analogue D-glutamate to form ternary complexes which can be distinguished by their different fluorescence properties. The affinity of the enzyme for NADPH diminishes with increases in pH or ionic strength of the solution. Experimental data obtained using modified glutamate dehydrogenases from mutant strains of N. crassa suggest that the reduced-coenzyme binding sites observed fluorimetrically are the same as those observed by enzyme kinetics." @default.
- W1966287972 created "2016-06-24" @default.
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- W1966287972 date "1975-02-01" @default.
- W1966287972 modified "2023-09-23" @default.
- W1966287972 title "Studies on the binary and ternary complexes formed by a neurospora glutamate dehydrogenase and its substrates" @default.
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- W1966287972 doi "https://doi.org/10.1016/0006-291x(75)90421-0" @default.
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