Abstract
The reactivity towards the monoclonal antibody (MAb) against bovine lactoferrin C-lobe was compared with six members of the transferrin family of proteins by ELISA and dot-blotting methods. This MAb recognizes WNIPMGL (467-473) of the bovine lactoferrin sequence. Human lactoferrin, Korean native goat lactoferrin and bovine transferrin showed weak reactivity with anti-C-lobe MAb. Human transferrin and ovotransferrin did not react with this antibody. As human lactoferrin in the denatured state showed reactivity with the antibody by ELISA, the configurational features of bovine lactoferrin and human lactoferrin were compared. It is observed that human lactoferrin epitopic site is covered with the bulky group and becomes exposed after denaturation.
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