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- W2017494087 abstract "Sloutions of (35S)bromosulphthalein ((35S)BSP) in heparinized canine plasma, in the proportions established in vivo after injecting BSP intravenously to test liver function, were ultracentrifugated at 226,000 g for 24 hr at 5 degrees. Protein-free supernatant was replaced by Krebs-Ringer buffer (pH 7.40), the protein sediment resuspended, and the mixture recentrifugated. That process was repeated several times, and the radio-activity of each resulting supernatant was measured. Since (35-S)BSP could not be adequately purified, supernatant radioactivities reflected both (35-S)BSP and radioimpurity. Therfore, a model was derived that (i) interpreted the rapid decrease in supernatant radioactivities of initial centrifugations and the gradual fall therafter; and (ii) allowed us to determine picomoles of non-protein-bound (35-S)BSP. Results indicated that only 0.053% (SD .0013%) of BSP in our system was not protein-bound." @default.
- W2017494087 created "2016-06-24" @default.
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- W2017494087 date "1975-03-01" @default.
- W2017494087 modified "2023-09-24" @default.
- W2017494087 title "A Model for Ultracentrifugal Quantification of [35S]Bromosulphthalein-Binding to Plasma Proteins in the Presence of Radioimpurities" @default.
- W2017494087 doi "https://doi.org/10.3181/00379727-148-38617" @default.
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