Cloning and sequencing of a cDNA encoding human milk β-casein

Bo Lönnerdal, Sven Bergström, Yvonne Andersson, Karin Hjalmarsson, Anna Karin Sundqvist, Olle Hemell

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


A cDNA of 1065 bp encoding the human milk β-casein was cloned and sequenced using a synthetic oligodeoxyribonucleotide probe and a human mammary gland library. The nucleotide (nt) sequence contained an open reading frame sufficient to encode the entire amino-acid (aa) sequence of a β-casein precursor protein consisting of 210 aa and a signal peptide of 15 aa. The nt sequence shows 45-62% homology to those of bovine, ovine, rat, and mouse β-caseins. The highly phosphorylated site, which is responsible for the calcium-binding capacity of β-casein, the signal peptide, and a sequence encoding for an inhibitor to the angiotensin-converting enzyme seem highly conserved among the β-caseins with known sequences.

Original languageEnglish (US)
Pages (from-to)153-156
Number of pages4
JournalFEBS Letters
Issue number1
StatePublished - Aug 20 1990


  • Angiotensin-converting enzyme inhibitor
  • Calcium-binding site
  • Human milk protein
  • Nucleotide sequence
  • Sequence comparison

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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