Spleen antibacterial peptides: high levels of PR-39 and presence of two forms of NK-lysin

Cell Mol Life Sci. 1999 Oct 1;56(1-2):174-8. doi: 10.1007/s000180050016.

Abstract

Antibacterial peptides were isolated from porcine spleen by acetic acid extraction, ion exchange chromatography and reverse-phase high-performance liquid chromatography. C-terminal ladder sequence analysis of a bioactive peptide with matrix-assisted laser desorption/ionization mass spectrometry after digestion with carboxypeptidases P and Y showed that it is identical to the antibacterial proline/arginine-rich intestinal peptide PR-39. It is present at high levels in granulocytes of the spleen, and peptides with C-terminal proline amide and internal adjacent Pro residues can be analyzed with this method. In addition, two forms of NK-lysin (NKL) were found. One, NKLi, is identical to that isolated from pig intestine, and the other, NKLbw, to a mature peptide deduced from a clone from a porcine bone marrow cDNA library.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Bacterial Agents / biosynthesis*
  • Anti-Bacterial Agents / chemistry
  • Antimicrobial Cationic Peptides / biosynthesis
  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / isolation & purification
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Enzyme-Linked Immunosorbent Assay
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Proteolipids / chemistry
  • Pulmonary Surfactants / chemistry
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Spleen / metabolism*
  • Swine

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • NK-lysin
  • Peptides
  • Proteolipids
  • Pulmonary Surfactants
  • PR 39