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Partial purification of a binding protein for polychlorinated biphenyls from rat lung cytosol: Physicochemical and immunochemical characterization

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00420a047· OSTI ID:6831838
; ;  [1]
  1. Huddinge University Hospital (Sweden)
A binding protein for certain methyl sulfone metabolites of polychlorinated biphenyls (PCB) was partially purified from lung cytosol of untreated female rats. The protein has an M{sub r} of 13,000 and a pI of 5.3 in the absence of reducing agents. In the presence of dithioerythreitol or {beta}-mercaptoethanol, the protein is split into subunits with a more basic pI. The 13-kDa protein was electroeluted from SDS-polyacrylamide gels, and an antiserum against the protein was raised in rabbit. The immunoglobulin fraction was shown to contain monospecific antibodies against the 13-kDa protein as determined by Western immunoblots. Due to striking similarities in physicochemical characteristics of the 13-kDa protein and a protein purified from rabbit lung and uterus, uteroglobin, the anti 13-kDa protein antibodies were tested for cross-reactivity. As judged by Western immunoblots, the anti 13-kDa protein antibodies did not cross-react with uteroglobin and the two proteins, although similar, do not seem to be identical. The 13-kDa protein is proposed to be responsible for the accumulation of certain methylsulfonyl-PCBs in lung tissue of rats. Monospecific antibodies against the 13-kDa protein should constitute immunochemical probes of great value in attempts to elucidate the physiological role of the protein as well as its possible role in PCB-induced respiratory toxicity.
OSTI ID:
6831838
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 27:20; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English

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