Abstract
Extracts from epithelial cells, seven successive concentric layers of the cortex, and the nucleus of calf lenses were submitted to gel chromatography on agarose Bio-Gel A-5m. In the mentioned order, corresponding to increasing age of the relevant lens cells, the content of α-crystallin in these extracts decreased significantly whereas the content of a very high-molecular weight fraction, resembling an aggregate composed of the polypeptide chains of α- and β-crystallin, increased markedly. The sedimentation coefficients of the α-crystallin preparations at concentrations of 0·8 mg/ml ranged from 17 to 21 S and passed through a minimum. Gel electrophoresis in polyacrylamide containing 6 m urea revealed significant changes in polypeptide composition. Nevertheless, no clear relation between sedimentation coefficients and polypeptide composition was found. Evidence has been obtained for the interaction of α-crystallin with constituents of β-crystallin which may lead to the formation of very high-molecular, finally insoluble aggregates.
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