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- W2005753280 abstract "The pKa's of dye conjugates of a series of proteins (gelatin, protamine, insulin, lysozyme, ribonuclease, trypsinogen, β-lactoglobulin, ovalbumin, bovine serum albumin) have been determined. In general the shift in pKa increases with increasing molecular weight. Gelatin, however, behaves in a unique way in that apolar interactions are weak. However, this is not due to its denatured condition, for random-coil polyvinylpyrrolidone conjugates show a large shifts in pKa. In all cases examined, urea abolishes the masking of the conjugated dye by the protein or polymer. The dependence of ΔpKa on molecular weight of the protein as well as the effects of urea have been interpreted in terms of the participation of ordered water (hydrotactoids) in interaction between apolar groups." @default.
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- W2005753280 date "1964-04-01" @default.
- W2005753280 modified "2023-09-27" @default.
- W2005753280 title "Ionic equilibria in protein conjugates: Comparison on proteins" @default.
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- W2005753280 doi "https://doi.org/10.1016/0304-4165(64)90165-5" @default.
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