Slingsby C, Bateman O A
Birkbeck College, Department of Crystallography, London, U.K.
Exp Eye Res. 1990 Jul;51(1):21-6. doi: 10.1016/0014-4835(90)90165-q.
Bovine beta-crystallin aggregates, beta H-, beta L1- and beta L2-crystallins, prepared by rapid gel filtration, are each subjected to anion-exchange chromatography in deaggregating media using a Pharmacia Fast Protein Liquid Chromatography System. beta B1, beta B2 and beta A4 subunits are rapidly isolated using a one step Mono Q column from beta H-, beta L2- and beta L1-crystallin, respectively. beta B3 and beta A3 are separated from each other using a second Mono Q column starting from beta L2- and beta L1-crystallin respectively. Whereas beta B2, beta B3 and beta A4 are common to all sizes of aggregate, beta B1 is restricted to beta H-crystallin and beta A3 is absent from beta L2-crystallin.
