The structure and properties of human beta-lipoprotein and beta-apoprotein Academic Article uri icon

Overview

MeSH Major

  • Blood Proteins
  • Lipoproteins

abstract

  • 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. © 1968.

publication date

  • June 10, 1968

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 4969860

Additional Document Info

start page

  • 699

end page

  • 705

volume

  • 31

number

  • 5