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- W992927090 abstract "This chapter discusses the radiation inactivation analysis of Na, K-ATPase. Radiation inactivation is a well-established technique for determining the molecular weights of both soluble and membrane-bound enzymes. The method involves irradiation of samples with sparsely ionizing radiation and works best for the enzymes of known molecular weight. The quantitation of results normally involves empirical calibration by irradiating enzymes of established molecular sizes. Irradiation artifacts can involve temperature, free radical, and scavenger effects, and samples are usually lyophilized and irradiated in vacuo at 0–40°C. Results from the irradiation of kidney microsome Na, K-ATPase and the two partial reactions, namely—K-pNPPase and Na-ATPase are presented in the chapter. Irradiation in the presence of ligands did not affect the target size. Measurement of kinetics on samples irradiated with 6 Mrad did not show any differences from the control. The chapter concludes that irradiation inactivation analysis of Na, K-activated ATPase activity gives simple results consistent with an apparent molecular weight around 260,000. This is in good agreement with some ultracentrifugal data, and although subject to some theoretical criticism, is certainly too large to be accommodated with in current values for an α, β-subunit, even taking account of bound carbohydrate." @default.
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- W992927090 date "1983-01-01" @default.
- W992927090 modified "2023-09-26" @default.
- W992927090 title "Radiation Inactivation Analysis of Na,K-ATPase" @default.
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- W992927090 doi "https://doi.org/10.1016/s0070-2161(08)60562-6" @default.
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