Interactions between bacterial pyrogen and proteolipid extracted from the cerebrum (II).

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Abstract
Cerebral proteolipid inactivation of the pyrogenicity of [Escherichia coli] lipopolysaccharide (LPS) in vitro was studied by Sephadex LH-20 column chromatography. When rabbit cerebral proteolipid was chromatographed, 2 main protein peaks were obtained. One appeared in the chloroform (C)/methanol (M) 6:1 and the other C/M 4:1 effluent, designated as fraction IV and fraction V, respectively. When the incubation mixture of proteolipid and LPS was chromatographed, a new protein peak appeared in the C effluent. The new protein peak was suggested to be a complex of proteolipid protein and LPS because pyrogenicity was detected in the protein fractions only after treatment with 2% SDS [sodium dodecyl sulfate]. Fraction V but not fraction IV inactivated the pyrogenicity of LPS in vitro. By rechromatography of the incubation mixture of fraction V and LPS, a complex of protein and LPS was also eluted in the C effluent. By rechromatography of the incubation mixture of fraction IV and LPS, such a complex was not detected in the C effluent. The proteolipid apoprotein eluted in the C/M 4:1 effluent on a Sephadex LH-20 column may play an important role in the inactivation of the pyrogenicity of LPS.

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