Secretory PAF-acetylhydrolase of the rat hepatobiliary system: characterization and partial purification.

@article{Svetlov1998SecretoryPO,
  title={Secretory PAF-acetylhydrolase of the rat hepatobiliary system: characterization and partial purification.},
  author={Stanislav I. Svetlov and Katherine M. Howard and Michael S Debuysere and Merle S. Olson},
  journal={The American journal of physiology},
  year={1998},
  volume={274 5 Pt 1},
  pages={G891-900}
}
Hepatocytes and Kupffer cells in primary culture both secrete plasma-type platelet-activating factor-acetylhydrolase (pPAF-AH) into serum-free culture medium. The rate of secretion of pPAF-AH by Kupffer cells was 20 to 25 times higher than from hepatocytes, and Kupffer cells expressed a higher level of pPAF-AH mRNA than did hepatocytes. Purified liver cell-secreted pPAF-AH exhibited a major protein band of 65-67 kDa on SDS-PAGE; this was the band predominantly labeled when the enzyme catalytic… CONTINUE READING

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