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- W2040886321 abstract "The process of the adsorption of proteins at the liquid/solid interface was investigated utilizing enzymes to indicate both the binding amounts and the extent of conformational alterations. Isotherms exhibiting (a) total amount bound, (b) amount bound in the inactive form, and (c) amount bound in the active form to a hydrophobic surface are given for a series of four enzymes (horseradish peroxidase, alkaline phosphatase, catalase, β-galactosidase). The results demonstrate that at low relative initial enzyme concentrations, enzyme adsorbs and is subsequently altered in conformation while at relatively high intitial enzyme concentrations, enzyme tends to adsorb and remain in its native, active conformation. This suggests a partitioning of an intermediate to either an active or an inactive state. Results of temperature and time studies are included which (a) help to define the reversibility of the various steps of the interaction and (b) characterize the conformational change as endothermic. Competition and sequential-addition studies help define better the extent of these resulting structural alterations and the effects of enzyme physical properties on these changes. The adsorption of enzyme onto various hydrophobic and hydrophilic surfaces was investigated with the results comfirming an increased tendency toward enzyme inactivation by the lower energy surfaces." @default.
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- W2040886321 date "1988-01-01" @default.
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- W2040886321 title "Conformational states of enzymes bound to surfaces" @default.
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- W2040886321 doi "https://doi.org/10.1016/0021-9797(88)90402-x" @default.
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