Purification and primary structure of murine cryptdin-1, a Paneth cell defensin

FEBS Lett. 1992 Jun 15;304(2-3):146-8. doi: 10.1016/0014-5793(92)80606-h.


We have purified and determined the amino acid sequence of cryptdin-1, a murine Paneth cell defensin. The peptide corresponds to a previously characterized mRNA that accumulates to high abundance during postnatal ontogeny of the small bowel. Acid-extracted intestinal protein was fractionated by cation-exchange chromatography and fractions were assayed for antimicrobial activity. One peak of anti-Salmonella activity contained a putative defensin, based on its predicted electrophoretic migration in acid-urea PAGE. The peptide was purified to homogeneity by RP-HPLC and sequenced. These studies demonstrate defensin expression in non-myeloid tissue. The N-terminal extension of cryptdin-1 is a unique structural feature of this novel epithelial defensin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Consensus Sequence
  • Ileum / chemistry*
  • Intestinal Mucosa / chemistry*
  • Jejunum / chemistry*
  • Male
  • Mice
  • Molecular Sequence Data
  • Protein Precursors / chemistry*
  • Protein Precursors / isolation & purification
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Sequence Homology, Nucleic Acid


  • Protein Precursors
  • Proteins
  • cryptdin