@article{11291,
  keywords = {Animals, Chromatography, Gel, Chromatography, Ion Exchange, Granuloma, Inflammation, Isoenzymes, Mice, Mice, Inbred C57BL, Molecular Weight, Mycobacterium Infections, Mycobacterium lepraemurium, Pancreatic Elastase, Protease Inhibitors},
  author = {Hsu P S and Izaki S and Hibino T and Izaki M},
  title = {Elastase activity in granulomatous inflammation in experimental murine leprosy.},
  abstract = {<p>Proteolytic activity for [3H]elastin, pyro-Glu-Pro-Val-pNA(S-2484), and Suc-(Ala)3-pNA(AAApNA) was demonstrated in the bound fraction extracted with 2 M KSCN + 0.1% Triton X-100 from hypersensitivity-type murine lepromas in C57BL/6N mice, while elastase-inhibitor activity was separately observed in the soluble fraction extracted with a Tris-saline buffer. Sephacryl S-200 gel chromatography showed a peak of elastolytic activity with approximately 20,000 in molecular weight. The following DEAE-Sepharose chromatography demonstrated three fractions of elastolytic activity (E-I, II, III). The inhibitory profile showed that E-I is a thiol proteinase, while E-II and E-III belong to serine proteinase-type elastases. Both E-II and E-III showed different properties with neutrophil elastase or elastase secreted from cultured macrophages, but identical characteristics to membrane bound-type elastase of monocytes. A lower level of elastolytic activity was detected in the bound fraction of nonhypersensitivity-type murine lepromas in CBA/N mice, suggesting a more involvement of membrane bound-type elastase from monocytes/macrophages during the tissue remodelings of hypersensitivity-type granulomas.</p>},
  year = {1986},
  journal = {Experimental and molecular pathology},
  volume = {45},
  pages = {84-92},
  month = {1986 Aug},
  issn = {0014-4800},
  doi = {10.1016/0014-4800(86)90009-2},
  language = {eng},
}