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

First Author  Ouellette AJ Year  1992
Journal  FEBS Lett Volume  304
Issue  2-3 Pages  146-8
PubMed ID  1618314 Mgi Jnum  J:1458
Mgi Id  MGI:49985 Doi  10.1016/0014-5793(92)80606-h
Citation  Ouellette AJ, et al. (1992) Purification and primary structure of murine cryptdin-1, a Paneth cell defensin. FEBS Lett 304(2-3):146-8
abstractText  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.
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