Abstract
In an attempt to resolve the present controversy concerning the reported presence of δ-crystallin in preparations of chick lens plasma membranes, a study was conducted on the extractability of chick lens fiber cell plasma membranes in the presence or absence of calcium ions. One lens from each animal was homogenized in calcium-containing buffer and the other in (calcium) chelating buffer. Each resulting water insoluble crude cell membrane fraction was evenly divided and membranes isolated from each portion by treatment with urea in either calcium-containing buffer or chelating buffer. The isolated membranes were analyzed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE). Gels of membranes isolated in the presence of calcium showed very prominent δ-crystallin bands while gels of membranes isolated under chelating conditions showed a marked depletion of δ-crystallin. The treatment sequence employed ruled out the possibility that the observed binding of δ-crystallin to the membranes was a result of a spurious association caused by calcium because excess soluble δ-crystallin was removed in discarded chelating buffer washes prior to the isolation of the membranes with urea in chelating buffer. The results of the study showed that δ-crystallin is an extrinsic protein of the chick lens fiber cell plasma membranes, and that its linkage to the membranes is calcium-dependent.
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