Polymorphonuclear leukocytes, when properly stimulated in vitro (1, 2), release an endogenous pyrogen that is believed to play a central role in the pathogenesis of fever (3,4). Demonstration that the release process is proroundly affected by factors involving electrolyte transport (2, 5) has suggested that the pyrogen may be derived from the membranes of the stimulated ceils (s).Previous studies on the nature of rabbit leukocytic pyrogen (6, 7) have revealed that it is: (a) nondialyzable, (b) relatively heat-labile, (c) precipitable with perchloric acid (HC104), (d) destroyed by phenol, (e) solublein 50 % methanol and 33 % saturated ammonium sulfate, (f) unaffected by butanol treatment, (g) inactivated by both diisopropyl fluorophosphate (DFP) and dinitrofluorobenzene (DNFB), and (h) rendered inert by trypsin and pepsin. These properties collectively indicate that it contains an essential protein.Approximately 50-fold purification of the crude pyrogen was first achieved by butanol treatment, removal of extraneous protein by methanol precipitation and anionic exchange chromatography (DEAE), and precipitation with ttCI04 (6). A later modification of the procedure (8) led to a further 4-fold purification and separated the activity of the pyrogen from that of lysozyme, an enzyme known to be released under the same conditions from polymorphonuclear leukocytes (2).Better methods of obtaining and purifying the pyrogen have since been devised, and further studies on its chemistry have been undertaken.
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