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Irreversible binding of bacteriophage T5 to its FhuA receptor protein is associated with covalent cross‐linking of 3 copies of tail protein pb4
Author(s) -
Feucht Andrea,
Heinzelmann Gerrit,
Heller Knut J.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81140-8
Subject(s) - covalent bond , bacteriophage , biophysics , receptor , chemistry , structural protein , binding protein , protein structure , biochemistry , microbiology and biotechnology , biology , gene , organic chemistry , escherichia coli
Irreversible 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.