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JULES FRANCOIS, M.D.; MARCEL RABAEY, M.D.

AMA Arch Ophthalmol. 1957;57(5):672-680.

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

Since the investigations of Mörner,¹² Krause,¹¹ and Schaeffer and Murray¹³ it has generally been accepted that in the eye lens of the cow there exist three water-soluble proteins, the -β, and -crystallins. The last one is found in very small concentration, less than 2% of the total protein (Table 1) and can be considered a residual protein, remaining in solution after maximal precipitation of the -and β-crystallins.

Even if the -crystallin is really a distinct protein, it would hardly be disclosed by electrophoresis, as it only amounts to less than 2%, and we could omit it in this work from our considerations.

As we have already shown previously (1953), paper electrophoresis reveals in the bovine lens three protein fractions existing in high concentrations: 1. Fraction I, the most rapidly moving component, corresponds to -crystallin, the purity of which we have ascertained in an investigation as yet unpublished. . . . [Full Text PDF of this Article]

Author Affiliations
Ghent, Belgium

From the Ophthalmological Clinic of the University of Ghent; Director: Prof. J. François. Qualified Research Worker of the "Fonds National de la Recherche Scientifique" (Dr. Rabaey).

Footnotes
Received for publication Oct. 24, 1956.

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