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• W2021446106 abstract "1.|The hydrogen ion equilibria of β-casein-B have been examined in the pH range 2.8 to 11.5. The effect of KCl, CaCl2, urea and temperature in the range 8 to 40 °C on the titration of the protein was determined. 2.|In the absence of urea, non-reversible or pathway-dependent behaviour was observed near the isoelectric point (approx. pH5) of the protein, indicating the importance of protein conformation on the observed titration curve. 3.|The changes in the titration curve obtained in the presence of CaCl2 may be interpreted as a combination of suppression of the protonation of the phosphoserine residues of the protein and large changes in protein conformation near the iso-electric point as Ca2+ is released from the protein. 4.|Spectrophotometric titration of the protein tyrosines showed that all four residues were available to the solvent. A value of 0.023 for w, the electrostatic factor, suggests that in the region pH 9–12 β-casein is unlikely to exist as either a globular protein or as a random coil. 5.|Comparison of the present results with those of α-casein showed that α- and β-casein are very similar in their titration properties." @default.
• W2021446106 created "2016-06-24" @default.
• W2021446106 creator A5040749308 @default.
• W2021446106 date "1972-07-01" @default.
• W2021446106 modified "2023-10-18" @default.
• W2021446106 title "Hydrogen ion equilibria of bovine β-casein-B" @default.
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• W2021446106 doi "https://doi.org/10.1016/0005-2795(72)90198-5" @default.
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