Bovine beta-lactoglobulin H: isolation by preparative isoelectric focusing in immobilized pH gradients and preliminary characterization

J Biochem Biophys Methods. Jun-Jul 1988;16(2-3):205-14. doi: 10.1016/0165-022x(88)90031-0.


In spite of the fact that beta-lactoglobulin (beta-lg) was first discovered in bovine milk more than fifty years ago, and that it represents the main whey protein component in all the milks in which it has been found, its biological role and genetic evolution still remain rather uncertain. From comparative studies of the primary and tertiary structures of beta-lg and of other proteins of a similar size, the existence of a new superfamily of proteins with the function of transporter of hydrophobic molecules has been conjectured. The elucidation of the structure of beta-lg either from different species or from different genetic variants of the same species should give useful information on the evolution and function of this protein family. With this aim in mind we have now undertaken the isolation and characterization of a recently discovered, new genetic variant of bovine beta-lg. A two-step purification procedure involving preparative HPLC gel filtration and preparative IEF-IPG has been successfully carried out; it affords a good recovery of the new beta-lg in highly purified form.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Agar Gel
  • Electrophoresis, Cellulose Acetate
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing*
  • Lactoglobulins / isolation & purification*
  • Milk Proteins / isolation & purification


  • Amino Acids
  • Lactoglobulins
  • Milk Proteins