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- W2094084978 abstract "Abstract The introduction of a long hydrocarbon chain between the Sepharose backbone and the competitive inhibitor of the enzyme inosinic acid 5′-monophosphate dehydrogenase, GMP, seems to have a profound effect on the binding of the enzyme to the derivative. The strongly bound enzyme could be eluted by the use of 3 m urea. Analytical gel electrophoresis showed six bands of protein corresponding to activity and electrophoresis in presence of sodium dodecyl sulphate gave a single band that has a molecular weight of 54,000. The enzyme was found to be readily renatured following denaturation with urea, guanidine-HCl, and SDS." @default.
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- W2094084978 date "1975-01-01" @default.
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- W2094084978 title "Inosinic acid 5′-monophosphate dehydrogenase of Escherichia coli: Purification by affinity chromatography and some properties" @default.
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- W2094084978 doi "https://doi.org/10.1016/0003-9861(75)90152-6" @default.
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