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.
Zhang
W Z
WZ
National Vision Research Institute of Australia, Carlton, Vic.
Augusteyn
R C
RC
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000375:Aging / Q000502:physiology; D000818:Animals; D002386:Cataract / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D003459:Crystallins / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism*
D003459:Crystallins