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- W1555940430 abstract "Publisher Summary This chapter presents the protocol for the measurements of protein interactions mediated by small molecules using sedimentation velocity that incorporates the several precautions that must be taken to ensure the validity of the fractionation test for distinguishing between ligand-mediated interaction and inherent heterogeneity; relatively concentrated solutions of protein are subject to ultracentrifugation several times. In the case of zone sedimentation in the preparative ultracentrifuge, several samples of protein from each peak are collected and pooled. For moving-boundary sedimentation in the analytical instrument, a Yphantis–Waugh partition cell is used to collect several samples of the slower moving peak, which are pooled. Each fraction is then reconcentrated by ultrafiltration; reeqnilibrated against buffer by rapid dialysis or by passage through a Sephadex G-25 column equilibrated with buffer and analyzed in the ultracentrifuge. A comparison experiment is made with the unfractionated material at the same concentration. For interactions, the fractions behave like the unfractionated material and show two peaks, whereas for heterogeneity a single peak is obtained." @default.
- W1555940430 created "2016-06-24" @default.
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- W1555940430 date "1978-01-01" @default.
- W1555940430 modified "2023-10-14" @default.
- W1555940430 title "[11] Measurements of protein interactions mediated by small molecules using sedimentation velocity" @default.
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- W1555940430 doi "https://doi.org/10.1016/s0076-6879(78)48013-9" @default.
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