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  Vol. 61 No. 3, March 1959 TABLE OF CONTENTS
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Agar Microelectrophoresis at High Tension of Soluble Lens Proteins

J. FRANCOIS, M.D.; M. RABAEY, M.D.

AMA Arch Ophthalmol. 1959;61(3):351-360.

Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

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 ({alpha}-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 . . . [Full Text PDF of this Article]


Author Affiliations

Ghent, Belgium

From the Ophthalmological Clinic of the University of Ghent, Prof. J. François, M. D., Director.


Footnotes

Submitted for publication Aug. 19, 1958.



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