On the presence of guanosine phosphate in the tail of bacteriophage T4.
Treatment of gp18, a biologically active monomer of the structural protein of the bacteriophage T4 contractile sheath, with 0.6 M-HClO4 leads to the release of GDP, GMP and inorganic phosphate. Each gp18 molecule is shown to carry three atoms of phosphorus. In the isolated protein preparation, gp18 and the nucleoside phosphate are in equimolar relation. It is suggested that in the native sheath-protein subunit, GDP and inorganic phosphate are united as GTP.
D002855:Chromatography, Thin Layer; D006150:Guanine Nucleotides / Q000032:analysis*; D006153:Guanosine Diphosphate / Q000032:analysis; D006157:Guanosine Monophosphate / Q000032:analysis; D006160:Guanosine Triphosphate / Q000032:analysis; D010710:Phosphates / Q000032:analysis; D013053:Spectrophotometry; D013604:T-Phages / Q000032:analysis*; D014764:Viral Proteins; D017376:Viral Tail Proteins
D006150:Guanine Nucleotides; D010710:Phosphates; D014764:Viral Proteins; D017376:Viral Tail Proteins; D006153:Guanosine Diphosphate; D006157:Guanosine Monophosphate; D006160:Guanosine Triphosphate