The concentration-dependent aggregation behaviour of purified ox liver and brain glutamate dehydrogenase preparations was compared with that of commercially-obtained preparations of the liver enzyme, which have recently been shown to have suffered proteolytic cleavage. Although there were no significant differences in these effects, the presence of 3 mM-GTP and 3 mM-NADH had markedly different effects on the two types of preparation. In this situation, at higher protein concentrations the commercially obtained preparations existed in a higher degree of aggregation than those which had not suffered proteolysis. Studies of the effects of GTP and NADH concentrations on the sedimentation coefficients at a fixed enzyme concentration suggested these effects to be largely due to differences in the affinities of the two preparations for nucleotides.
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Research Article| October 01 1981
Sedimentation properties of native and proteolysed preparations of ox glutamate dehydrogenase
Biochem J (1981) 199 (1): 235–238.
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A D McCarthy, P Johnson, K F Tipton; Sedimentation properties of native and proteolysed preparations of ox glutamate dehydrogenase. Biochem J 1 October 1981; 199 (1): 235–238. doi: https://doi.org/10.1042/bj1990235
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