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A single step column procedure for the separation of chick lens soluble proteins is described. α-, β- and δ-crystallin, which account for 80–90% of the soluble protein are separated using this technique, with little or no cross-contamination between classes, as judged by immuoelectrophoresis. Analysis of the fractions in sodium dodecylsulphate-polyacrylamide (SDS) and isoelectric focusing (IEF) gels in dissociating conditions identifies and characterizes the major α-, β- and δ-crystallin subunits. Fresh lenses from day-old chicks were labelled by culturing in medium containing radioactive amino acids and the synthesis of individual crystallin subunits analysed. In both pulse and pulse-chase labelled lenses at least 70% of the incorporated radioactivity could be assigned to characterized crystallin subunits. Differences were observed in the radioactivity profiles from pulse and pulse-chase labelled lenses when analysed on SDS and IEF gels and some polypeptides showed labelling characteristics typical of post-translational modifications of existing protein chains.

Preliminary studies on distributions of attached algae in British estuaries suggest that the estuaries might be classified on the basis of the flora in the upper reaches. This could contribute to biological assessment of water quality in estuaries.