Immunochemical studies on the evolution of tryptophanase and the two subunits of tryptophan synthetase of Escherichia coli K 12

Chaffotte, A.F.; Zakin, M.M.; Goldberg, M.E.

Biochemical and Biophysical Research Communications 92(2): 381-388

1980


ISSN/ISBN: 0006-291X
PMID: 6986866
DOI: 10.1016/0006-291x(80)90344-7
Accession: 043330052

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Abstract
In order to test if the α and β2 subunits of tryptophan synthetase and tryptophanase, three proteins involved in the metabolism of tryptophan in Escherichia coli K 12, have some common structural features reflecting an evolutionary filiation, an immunochemical comparison of these enzymes has been made using antibodies directed against either the native or the denatured β2 protein. The lack of cross-reactivity observed in the case of the three proteins studied, even when in their denatured state, suggests that, despite their functional relationships, they probably do not derive from a common ancestor.