TY - JOUR
T1 - The structure and properties of human beta-lipoprotein and beta-apoprotein
AU - Gotto, A. M.
AU - Levy, R. I.
AU - Rosenthal, A. S.
AU - Birnbaumer, M. E.
AU - Fredrickson, D. S.
PY - 1968/6/10
Y1 - 1968/6/10
N2 - Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein (Granda and Scanu, 1966) or a chemical derivative of the apoprotein (Gotto et al., 1968a, b, c; Scanu et al., 1967; Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining.
AB - Little is known about the structure of the protein of serum beta-lipoprotein owing to the insolubility of the delipidated product (beta-apoprotein). Attempts have been made to solubilize the apoprotein (Granda and Scanu, 1966) or a chemical derivative of the apoprotein (Gotto et al., 1968a, b, c; Scanu et al., 1967; Shore and Shore, 1967). This communication describes the preparation of beta-apoprotein by solubilization with sodium decyl sulfate. The apoprotein closely resembles the parent lipoprotein in immunological properties and structural conformation. The circular dichroism and infrared spectrum of beta-lipoprotein indicate a significant amount of pleated sheet, anti-parallel chain (APC) β-structure. This is also true for the apoprotein, except that the molar ellipticity at 216 mμ ([θ′]216) is reduced by about 25%. The apoprotein has a fibrillar appearance when viewed with the electron microscope by the technique of negative staining.
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U2 - 10.1016/0006-291X(68)90618-9
DO - 10.1016/0006-291X(68)90618-9
M3 - Article
C2 - 4969860
AN - SCOPUS:0014409190
SN - 0006-291X
VL - 31
SP - 699
EP - 705
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 5
ER -