Isolation and characterization of a 21 kDa whey protein in Rhesus monkey (Macaca mulatta) milk

Clemens Kunz, Bo Lönnerdal

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A soluble protein in Rhesus monkey milk was isolated to apparent homogeneity by FPLC gel filtration, anion-exchange and reverse-phase chromatography. It is a major milk protein and is present at 2.5-3.0 mg/ml milk throughout lactation. It is only found in the whey fraction of milk; acid precipitation of casein does not result in any significant change in its concentration. A molecular weight (MW) of about 21.6 kDa was estimated from gel filtration and SDS gel electrophoresis and also calculated from its amino acid composition. The amino acid composition of this protein is similar to that of bovine β-lactoglobulin (β-Lg), but it is larger in size, possibly representing a family of primate β-Lgs.

Original languageEnglish (US)
Pages (from-to)463-469
Number of pages7
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume108
Issue number4
DOIs
StatePublished - 1994

Keywords

  • 21 kDa whey protein
  • Anion-exchange
  • FPLC
  • Gel filtration
  • Milk
  • Reverse-phase chromatography
  • Rhesus monkey

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

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