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Generation of polyclonal antibodies against a chemically synthesized N‐terminal fragment of the bacteriocin pediocin PA‐1
Author(s) -
Martínez M. I.,
Rodríguez J. M.,
Suárez A.,
Martínez J. M.,
Azcona J. I.,
Hernández P. E.
Publication year - 1997
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.1997.00157.x
Subject(s) - polyclonal antibodies , bacteriocin , fragment (logic) , antibody , bacteria , chemistry , microbiology and biotechnology , biology , biochemistry , stereochemistry , genetics , computer science , programming language
Six mice were immunized intraperitoneally (i.p.) with a chemically synthesized 9‐mer fragment (PH1) designed from the N‐terminal part of the bacteriocin pediocin PA‐1 and conjugated to keyhole limpet haemocyanin (KLH). After three doses of the immunogen had been administered, serum‐specific antibodies were detected by a competitive direct ELISA. Myeloma cells were injected i.p. into mice in order to obtain ascites polyclonal antibodies. Although four mice developed ascites, only mouse 2 had detectable specific antibodies in the ascites fluid. The serum and ascites antibodies were specific for PH1 but they did not recognize the whole pediocin PA‐1 molecule. This is the first attempt to generate antibodies against bacteriocins with a chemically synthesized oligopeptide as immunogen. This approach still remains attractive for detection, quantification, mode of action studies and purification of bacteriocins, especially those for which the purification process is difficult or inefficient at present.