On the antigenic relationship between the αA and αB subunits of α-crystallin in bovine lens

Abstract

The immunochemical reactivities of the αA and αB subunits from bovine α-crystallin have been compared using 5 monoclonal antibodies and 2 polyvalent antisera. Each subunit bound the same maximum amount of antibody, regardless of its source, and each subunit was able to completely displace α-crystallin from its antibodies. One monoclonal antibody (463–122) and mouse anti-αB polyclonal antiserum bound equally well to the two subunits; with the other monoclonal antibodies and an anti α-crystallin antiserum, the affinities for the αA chains were about 10³ fold higher than those for the αB chains. These observations indicate that the αA and αB subunits of bovine α-crystallin share several similar, but not necessarily identical, cross-reacting antigenic determinants. The reasons for the differences between these observations and those of other investigators are discussed.