Irreversible binding of bacteriophage T5 to its FhuA receptor protein is associated with covalent cross-linking of 3 copies of tail protein pb4

AbstractIrreversible binding of bacteriophage T5 to its FhuA receptor protein is characterized by a high activation energy, typical for reactions where covalent bonds are formed [Zarnitz, M.L. and Weidel, W. (1963) Z. Naturforsch. 18b, 276–280]. Upon binding of radiolabeled T5 phages to FhuA formation of a new protein of 250 kDa was observed. Using electrophoretical and Western blotting techniques this protein was shown to be formed by cross-linking of 3 copies of tail protein pb4, rather than by cross-linking of FhuA and the receptor-binding protein