The effect of guanidinium chloride on the self-association of bovine liver glutamate dehydrogenase: a gel filtration study.

The associative behaviour of bovine liver glutamate dehydrogenase has been studied by gel chromatography at neutral pH in 1 M guanidinium chloride and 1 M sodium chloride. In guanidinium chloride both the elution volume and the elution profile of the enzyme are independent of protein concentration, whereas in sodium chloride they are strongly dependent on it. In NaCl the enzyme behaves as expected according to the well established random association model, whereas in guanidinium chloride it appears to have completely lost the self-associative property. Furthermore, since the elution volume of the enzyme in guanidinium chloride corresponds to that of an hexamer, trimer formation reported to occur in these conditions is not confirmed by this technique.