Isolation and characterization of a novel 39 kilodalton whey protein from bovine mammary secretions collected during the nonlactating period

Biochem Biophys Res Commun. 1988 Jan 15;150(1):329-34. doi: 10.1016/0006-291x(88)90524-4.

Abstract

A 39 kilodalton glycoprotein has been isolated from bovine mammary secretions by heparin-agarose affinity chromatography and gel filtration. It is a minor whey protein in mammary secretions collected during the nonlactating period, but is clearly detectable by affinity chromatographic and immunoblotting techniques. It is not detectable by these techniques in milk or colostrum. This protein is not immunologically related to milk proteins, serum proteins or cytoskeletal proteins. The N-terminal amino acid sequence (36 amino acids) is not similar to other known proteins. Isolating this novel 39 kilodalton protein provides a specific marker for mammary function during the nonlactating period.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylglucosaminidase / metabolism
  • Animals
  • Cattle
  • Chromatography, Affinity
  • Chromatography, Gel
  • Colostrum / analysis
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Glycoproteins / isolation & purification
  • Immunodiffusion
  • Immunoenzyme Techniques
  • Mammary Glands, Animal / metabolism*
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
  • Milk / analysis
  • Milk Proteins / isolation & purification*
  • Molecular Weight
  • Whey Proteins

Substances

  • Glycoproteins
  • Milk Proteins
  • Whey Proteins
  • Acetylglucosaminidase
  • Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase