Fatty acids bound to vitamin D-binding protein (DBP) from human and bovine sera

Biochem Int. 1989 Jul;19(1):1-7.

Abstract

Human and bovine vitamin D-binding protein (DBP) have been isolated from serum by a method that does not involve denaturing steps. This method includes Cibacron Blue-Sepharose chromatography, gel filtration, DEAE-Sephadex chromatography and albumin immunoadsorption. Analysis of fatty acids bound to the isolated human and bovine DBP showed molar ratios of fatty acid to protein of 0.4 and 1.3 respectively meanwhile human and bovine albumin have bound 1.8 and 1.5 moles per mol respectively. Most of fatty acids bound to human and bovine DBP are monounsaturated and saturated, mainly oleic and palmitic acids, which together account for 50% of the total of fatty acids in both species. By contrast, polyunsaturated fatty acids represented a minor component, less than 5%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chromatography
  • Fatty Acids / analysis*
  • Fatty Acids / metabolism
  • Fatty Acids, Unsaturated / analysis
  • Humans
  • Immunosorbent Techniques
  • Oleic Acid
  • Oleic Acids / analysis
  • Oleic Acids / metabolism
  • Palmitic Acid
  • Palmitic Acids / analysis
  • Palmitic Acids / metabolism
  • Protein Binding
  • Serum Albumin / analysis
  • Serum Albumin / metabolism
  • Vitamin D-Binding Protein / analysis*
  • Vitamin D-Binding Protein / metabolism

Substances

  • Fatty Acids
  • Fatty Acids, Unsaturated
  • Oleic Acids
  • Palmitic Acids
  • Serum Albumin
  • Vitamin D-Binding Protein
  • Oleic Acid
  • Palmitic Acid