Abstract
A method is described for the isolation of a structural protein of the vitreous body, which has been named vitrosin. The analyses show that vitrosin is a viscous, thixotropic, fibrous protein. Electron micrographs reveal that vitrosin particles are long fibrils, averaging 250 A in width. The isoelectric point was found to be around pH 5.5 and the shrinkage temperature 60°C. Vitrosin is composed of a protein-carbohydrate complex. It contains cystine and the aromatic amino acids in low quantities. Hexosamine could not be detected in the complex.
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Selected References
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