Bacteriophage T4 gene 32 protein shares antigen determinants with reconstituted HeLa hnRNP proteins in western blots.
A polyclonal antiserum against purified bacteriophage T4 gene 32 protein was raised in rabbits. In Western blots it detected a number of SDS-PAGE separated nuclear and ribosomal proteins of HeLa cells. Using a renaturing blotting system, however, larger hnRNP proteins ranging between 66.000 and 82.000 Da preferentially reacted with this antiserum. In addition hnRNP group A core proteins were detected to a minor extent. Nucleic acid binding proteins like histones or ribosomal proteins were not stained by this antibody after renaturation.
Schenkel
J
J
Institut für Immunologie, Universität, Heidelberg, FRG.
Hovemann
B
B
D015153:Blotting, Western; D004268:DNA-Binding Proteins / Q000276:immunology* / Q000302:isolation & purification; D000939:Epitopes / Q000032:analysis*; D004926:Escherichia coli / Q000235:genetics; D006367:HeLa Cells / Q000032:analysis; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D006801:Humans; D007106:Immune Sera; D008970:Molecular Weight; D012261:Ribonucleoproteins / Q000276:immunology* / Q000302:isolation & purification; D013604:T-Phages / Q000235:genetics*; D014764:Viral Proteins / Q000276:immunology* / Q000302:isolation & purification
D004268:DNA-Binding Proteins; D000939:Epitopes; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D007106:Immune Sera; D012261:Ribonucleoproteins; D014764:Viral Proteins; C060035:gp32 protein, Enterobacteria phage T4