O. Kudela et al., CONFORMATIONAL-CHANGES IN PH2-TREATED HUMAN INTERFERON-ALPHA-2 DETECTED WITH MONOCLONAL-ANTIBODIES, Hybridoma, 15(3), 1996, pp. 185-189
Monoclonal antibodies allowed to demonstrate the existence of alternat
ive antigenic forms of the same molecule as of human interferon (IFN)-
alpha 2. Exposure of recombinant IFN to pH 2, although not affecting i
ts bioactivity, induced structural modulation of molecular surface, Th
e antigenic structure of IFN-alpha 2 appeared to be built of the acid-
stable and acid-labile epitopes, In general, the acid-stable sites det
ermined subtype-specific antigenic properties of the protein, whereas
the acid-labile determinants were responsible for antigenic characteri
stics shared by some other human IFNs. Acidification of IFN-alpha 2 to
on 2 for at least 1-2 h resulted in simultaneous structural rearrange
ment of all acid-labile sites.