Open AccessThe Antigenic Independence of the Three Aspartokinases of Escherichia coli K 12
Author(s) -
Kaminski M.,
FalcozKelly F.,
TruffaBachi P.,
Patte J.C.,
Cohen G. N.
Publication year - 1969
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1969.tb00770.x
Subject(s) - homoserine , threonine , escherichia coli , chemistry , biochemistry , agar gel , lysine , methionine , dehydrogenase , enzyme , antigen , biology , microbiology and biotechnology , serine , amino acid , gene , quorum sensing , genetics , virulence
The immunological properties of three pure enzyme proteins carrying respectively the two threonine‐sensitive aspartokinase I and homoserine dehydrogenase I activities (Aspartokinase I—homoserine dehydrogenase I), the two methionine‐repressible aspartokinase II and homoserine dehydrogenase II activities (aspartokinase II—homoserine dehydrogenase II), and the lysine‐sensitive aspartokinase III (aspartokinase III), have been investigated by means of double diffusion precipitation in agar gel. The antigenic structures of these three proteins appeared different: no cross‐reactions were detected.