Agar Microelectrophoresis at High Tension of Soluble Lens Proteins

Abstract

Hesselvik was the first to succeed, in 1939, in fractionating lenticular proteins by electrophoresis according to Tiselius. This method of investigation has since been used by numerous investigators studying the soluble proteins of the ocular lens, namely, Viollier, Labhart and Süllmann (1947), Smelzer and von Sallmann (1949), Lewis and Moses (1950), Bon (1955), Rao et al. (1955), Orekhovich (1957), and Bloemendal (1957). Fractionation has subsequently been perfected with the introduction of paper electrophoresis (d'Ermo, 1952; Croisy, 1952; François, Wieme, Rabaey, and Neetens, 1953; Stemmerman, 1953; Bon, 1955), and it soon became apparent that the protein composition of the lens is more complex than would be suggested by the classical schema with its three crystallins (α-crystallin, (β-crystallin, and albumin). A comparative study of results obtained by electrophoresis has shown, among other things, that in a great many animal species the number of protein constituents of the lens exceeds the three fractions