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Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins.

Publication ,  Journal Article
Jackson, RL; Lin, HU; Chan, L; Means, AR
Published in: Biochim Biophys Acta
February 20, 1976

High density lipoproteins were isolated from plasma of white Leghorn hens by ultracentrifugal flotation between densities 1.063 and 1.210 g/ml. After delipidation, the lipid-free proteins were fractionated by chromatography on Sephadex G-150 in urea; one major apolipoprotein was isolated and characterized. From its chemical, physical and immunochemical properties, the major apoprotein from hen high-density lipoproteins has characteristics similar to the major apoprotein of human high density lipoproteins, apoA-I. Thus the hen protein has been designated hen apoA-I. Hen apoA-I has a molecular weight of approximately 28 000 as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Its calculated molecular weight from its 234 constituent amino acids is 26 674. Hen apoA-I differed from its human counterpart by containing isoleucine. Treatment of hen apoA-I with carboxypeptidase A yielded a COOH-terminal sequence of Leu-Val-Ala-Gln. Automatic Edman degradation of the apoprotein gave an NH2-terminal sequence of Asp-Glu-Pro-Gln-Pro-Glu-Leu. Hen apoA-I had a circular dichroic spectrum typical of alpha-helical structures; the calculated helicity was 90%. Goat antisera prepared to hen apoA-I formed precipitin lines of complete identity to the hen apoprotein but lines of only partial identity to human apoA-I. These studies show that the major apoprotein from hen and human high-density lipoproteins have similar properties to each other suggesting a common physiologic function.

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Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

February 20, 1976

Volume

420

Issue

2

Start / End Page

342 / 349

Location

Netherlands

Related Subject Headings

  • Swine
  • Spectrophotometry
  • Species Specificity
  • Protein Conformation
  • Molecular Weight
  • Lipoproteins, HDL
  • Immunodiffusion
  • Humans
  • Circular Dichroism
  • Animals
 

Citation

APA
Chicago
ICMJE
MLA
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Jackson, R. L., Lin, H. U., Chan, L., & Means, A. R. (1976). Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins. Biochim Biophys Acta, 420(2), 342–349. https://doi.org/10.1016/0005-2795(76)90326-3
Jackson, R. L., H. U. Lin, L. Chan, and A. R. Means. “Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins.Biochim Biophys Acta 420, no. 2 (February 20, 1976): 342–49. https://doi.org/10.1016/0005-2795(76)90326-3.
Jackson RL, Lin HU, Chan L, Means AR. Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins. Biochim Biophys Acta. 1976 Feb 20;420(2):342–9.
Jackson, R. L., et al. “Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins.Biochim Biophys Acta, vol. 420, no. 2, Feb. 1976, pp. 342–49. Pubmed, doi:10.1016/0005-2795(76)90326-3.
Jackson RL, Lin HU, Chan L, Means AR. Isolation and characterization of the major apolipoprotein from chicken high density lipoproteins. Biochim Biophys Acta. 1976 Feb 20;420(2):342–349.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

February 20, 1976

Volume

420

Issue

2

Start / End Page

342 / 349

Location

Netherlands

Related Subject Headings

  • Swine
  • Spectrophotometry
  • Species Specificity
  • Protein Conformation
  • Molecular Weight
  • Lipoproteins, HDL
  • Immunodiffusion
  • Humans
  • Circular Dichroism
  • Animals