Abstract
Investigation of the migration of in vitro synthesized γ-crystallin which has not been heat denatured on polyacrylamide gel electrophoresis in presence of sodium dodecyl sulfate indicates that this class of proteins behaves in an anomalous manner. While other in vitro synthesized lens proteins under these conditions migrate as theoretically expected, γ-crystallin is retarded, having a mobility comparable to a 92 000 dalton component. Only upon heat denaturation does this protein fraction migrate as a 20 000 dalton species. Since other in vitro synthesized lens proteins have molecular weights of approximately 20 000 daltons, it is only with this methodology that γ-crystallin synthesis can be unequivocally followed in a simple, rapid, one-dimensional fractionation system.
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