[The role of the structural organization of apoprotein E in cholesterol binding].
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.
D001053:Apolipoproteins / Q000032:analysis* / Q000378:metabolism; D001057:Apolipoproteins E; D001120:Arginine / Q000032:analysis; D002352:Carrier Proteins / Q000032:analysis* / Q000378:metabolism; D002784:Cholesterol / Q000378:metabolism*; D006657:Histones / Q000032:analysis; D011487:Protein Conformation; D013053:Spectrophotometry
D001053:Apolipoproteins; D001057:Apolipoproteins E; D002352:Carrier Proteins; D006657:Histones; D001120:Arginine; D002784:Cholesterol
Rol' strukturnoĭ organizatsii apoproteina E v sviazyvanii kholesterina.