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- W2092119857 abstract "1.|Titration of α-lactalbumin in 0.15 M KCl from an initial pH of 5.7–6.1 to pH 2.0 results in a conformational change below pH 4.0 which gives rise to molecular expansion. Exposure of α-lactalbumin to pH values in the range 2.0–3.5 results in a new curve on back titration to higher pH, with time-dependent changes occurring above pH 5.0. The back titration and initial titration curves coincide near pH 6.0, indicating that changes occurring at lower pH are reversible at pH 6.0. 2.|The irreversibility of the initial titration curve in the pH range 3.5 to 6.0 is apparently not the result of irreversibility of the acid conformational change, but rather due to the slow rates of precipitation and solution of precipitated protein in this pH region. The magnitude of the electrostatic factor, w, is consistent with association of the protein at acid pH. 3.|The pKtint values of the carboxyl groups in 0.15 M KCl are somewhat low, and are not “normalized” in the denaturing guanidine urea solvent, indicating the probable presence of cationic groups adjacent to carboxyl groups in the primary structure. 4.|The alkaline portion of the titration curve in 0.15 M KCl is reversible from 5.7–6.1 to pH 12. Above pH 10.5 (25°) and pH 11.2 (10°), a conformational change occurs leading to expansion of the protein. This change appears to be less drastic than that occurring at acid pH." @default.
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- W2092119857 date "1967-01-01" @default.
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- W2092119857 title "Inter- and intramolecular interactions of α-lactalbumin VII. The hydrogen ion titration curve of α-lactalbumin" @default.
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- W2092119857 doi "https://doi.org/10.1016/0005-2795(67)90036-0" @default.
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