Direct identification and characterization of llama (Lama glama L.) whey proteins by microsequencing after western blotting

J Biochem Biophys Methods. 1990 Sep-Oct;21(3):227-36. doi: 10.1016/0165-022x(90)90016-6.

Abstract

Amino acid sequence determination is the most reliable and powerful tool to identify a protein or to classify a new one by comparison of its primary structure with already known sequences. A rapid and simple purification procedure is an essential pre-requisite for routine sequence determination. Structural characterization of llama whey proteins was undertaken for evolutionary as well as economic purposes. N-terminal sequence analyses directly on an immobilon polyvinylidene difluoride (PVDF) membrane, following Western blotting of both native and SDS-denatured llama whey proteins after polyacrylamide gel electrophoresis, revealed three different forms of glycosylated alpha-lactalbumin, and a protein with a high degree of homology with a camel whey protein of unknown function. Furthermore, by immunoblotting techniques, the electrophoretic band corresponding to serum albumin was identified.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Camelids, New World / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Lactalbumin / chemistry
  • Lactalbumin / isolation & purification
  • Milk Proteins / chemistry*
  • Milk Proteins / isolation & purification
  • Molecular Sequence Data
  • Serum Albumin / chemistry
  • Serum Albumin / isolation & purification
  • Species Specificity
  • Whey Proteins

Substances

  • Milk Proteins
  • Serum Albumin
  • Whey Proteins
  • Lactalbumin