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- W1541570420 abstract "Using the determination of an abrupt shift in absorbance corresponding to micelle formation of Triton X-100, the binding of this nonionic detergent to a number of soluble proteins was studied. In decreasing order, human albumin, bovine albumin, and β-lactoglobulin bound this detergent. Horse myoglobin, trypsin, human immunoglobulin G, casein partial digests, and neomycin did not. The mean detergent binding per mole protein was found to anomalously increase with decrease in protein concentration. Analysis of the premicellar limb slope of the Triton X-100 revealed a slope increase with human and bovine albumin, but not for β-lactoglobulin or for any of the proteins where binding was absent. The data suggest that the Triton X-100 is predominantly hydrophobically bound to certain proteins." @default.
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- W1541570420 date "1971-03-01" @default.
- W1541570420 modified "2023-09-29" @default.
- W1541570420 title "Interactions of a nonionic detergent" @default.
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- W1541570420 doi "https://doi.org/10.1016/0021-9797(71)90149-4" @default.
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