1. Immunological characterization of the low-molecular-weight DNA binding protein of mouse mammary tumor virus.
- Author
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Arthur LO, Long CW, Smith GH, and Fine DL
- Subjects
- Animals, Antigens, Viral, Cell Line, Chemical Precipitation, Chromatography, Affinity, Cross Reactions, Cytoplasm immunology, DNA, Viral metabolism, Electrophoresis, Polyacrylamide Gel, Epitopes, Female, Mice, Molecular Weight, Protein Binding, RNA Viruses immunology, Radioimmunoassay, Viral Proteins isolation & purification, Mammary Tumor Virus, Mouse immunology, Viral Proteins immunology
- Abstract
p14, a low-molecular-weight MMTV protein previously identified as having DNA-binding properties and encoded by the gag region of the MMTV genome, was purified by affinity chromatography on DNA-sepharose. Immunological characterization of the purified protein showed that MMTV p14 shares no cross-reactivity with gp52, gp36 and p10, antigens associated with the MMTV envelope, nor with p27 antigen found in the virion core. Purified MMTV p14 did show cross-reactivity with purified intracytoplasmic A particles, supporting the concept that A particles are morphological precursors to MMTV cores. In addition, shared antigenic determinants between intracytoplasmic A particles and MMTV p27, p20 and p10 were demonstrated. MMTV p14 did not cross-react with the low-molecular-weight DNA-binding proteins of MuLV or of type-C or -D viruses of higher mammals.
- Published
- 1978
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