Characterization of baboon (Papio hamadryas) milk proteins

A. J. Hall, A. Masel, K. Bell, J. A. Halliday, D. C. Shaw, J. L. Vandeberg

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The major proteins of baboon milk were identified as β-lactoglobulin (βLG), α-lactalbumin (αLA), lysozyme, lactoferrin, casein, and albumin by immobiline isoelectric focusing, SDS-PAGE, immunoblotting of gels with rabbit antisera to human αLA, lysozyme, and albumin and bovine βLG and casein, and N-terminal sequencing of proteins blotted from gels. The first 30 N-terminal residues of baboon βLG are identical to those of macaque (Macaca fasicularis) βLG except for a (D/N) polymorphism at residue 2. The complete cDNA sequence and derived amino acid composition of βLG were elucidated using RT-PCR amplification of poly(A)+ mRNA purified from lactating mammary gland. Baboon βLG consists of 168 amino acid residues (Mr 20, 750) and is the longest βLG identified to date. βLG and αLA polymorphisms with three (A, B, and C) and two (A and B) variants, respectively, were detected by immobiline IEF, pH 4-6, of individual baboon milk samples at varying stages of lactation.

Original languageEnglish (US)
Pages (from-to)59-71
Number of pages13
JournalBiochemical Genetics
Volume39
Issue number1-2
DOIs
StatePublished - 2001
Externally publishedYes

Keywords

  • Baboon
  • Milk
  • Polymorphism
  • cDNA
  • β-lactoglobulin

ASJC Scopus subject areas

  • Biochemistry
  • Ecology, Evolution, Behavior and Systematics
  • Molecular Biology
  • Genetics

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