Glutamate dehydrogenase purification

Walsh, P.J. (1981). Purification and characterisation of glutamate dehydrogenases from three species of sea anemones adaptation to temperature within and among species from different thermal environments. Marine Biology Letters 2,289-299. 

Inokuchi, R., Itagaki, T., Wiskich, J., Nakayama, K., and Okada, M. (1997). An NADP-glutamate dehydrogenase in the green alga Bryopsis maxima. Purification and properties. Plant Cell Physiol. 38, 327-335. 

Enzyme Concentration and Purification. The number of existing enzymes is estimated to be more than 10,000 of which more than 100 have been purified in crystalline form and over 600 in fairly purified form. The molecular weight of enzymes varies from 12,700 (ribonuclease) to over 1,000,000 (L-glutamate dehydrogenase, d-carboxylase). All enzymes are proteins, conjugated proteins or metalloproteins containing one or more active sites per molecule. 

Guanosine 5 -triphosphate (periodate oxidized) (21) Purification of glutamate dehydrogenase 84... 

The first demonstration of transhydrogenase activity in Pseudomonas fluoreacens by Colowick et al. (1) was carried out with a crude extract obtained from cells grown on citrate as the sole carbon source. This extract could be fractionated further by acetone precipitation followed by calcium phosphate adsorption and subsequent elution with potassium phosphate. A second acetone fractionation and calcium phosphate adsorption gave a total purification of about 200-fold. This preparation was devoid of dehydrogenase activity using glutamate, isocitrate, lactate,... 

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