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- W2023885145 abstract "A theory of isopycnic sedimentation of interacting systems provides a theoretical explanation for the isopycnic behavior of catalase and other proteins in metrizamide gradients of pH 7.0–7.5, particularly the bimodal banding patterns reported by some investigators. As for whether or not the model is realistic, a spectroscopic investigation provides an unambiguous demonstration of a reversible interaction between metrizamide and the catalase dimers formed by dissociation of catalase tetramer at pH 3. The metrizamide-catalase dimer complex(es) is of high bouyant density. In addition, metrizamide at pH 7.4 interacts with heat-denatured ovalbumin. These observations suggest that the denser band in the experimental bimodal isopycnic patterns might be a complex(es) of metrizamide with a comformationally altered state of the protein." @default.
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- W2023885145 date "1981-10-01" @default.
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- W2023885145 title "A combined theoretical and experimental study of the interaction of metrizamide with proteins" @default.
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- W2023885145 doi "https://doi.org/10.1016/0003-9861(81)90471-9" @default.
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