The ability of some proteins to bind cholesterol was accompanied by a decrease of turbidity of aqueous cholesterol suspensions and correlated with a quantity of arginine residues in them. Maximum clearing of aqueous cholesterol suspensions at the addition of proteins containing equimolar arginine concentrations was observed in the presence of apoproteins E and A-I. Optical rotatory dispersion spectra of apoprotein E, polyarginine and histone H3 have shown the influence of sterol on the secondary structure of apoprotein E only.
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