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On the interaction of alpha-crystallin with membranes.

The interaction of human and bovine alpha-crystallins with bovine lens membranes was evaluated using binding curves and Scatchard plots constructed from scans of SDS-PAGE gels and/or from the association of [14C]-leu alpha-crystallin with the membranes. No differences were observed for total bovine, normal human 19 and 88 year old and cataractous alpha-crystallins. In each case, interaction takes place through two distinct processes, a) a high affinity (Kd = 1 x 10(-8) M) binding with low capacity (25 mg alpha-crystallin/g membrane protein) and b) partitioning (Kp = 0.25 l/g membrane protein). Loss of the high-affinity binding component was observed for bovine nuclear alpha-crystallin. Contrary to previous reports, it is concluded that cataract formation does not affect the ability of human alpha-crystallins to interact with bovine lens membranes. Reanalysis of previously published data supports this conclusion.