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Incorporation of Glycine and Serine in the Proteins of Lenses Cultured in Vitro

FREDERIC C. MERRIAM, Ph.D.; V. EVERETT KINSEY, Ph.D.

Arch Ophthal. 1950;44(5):651-658.

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

PREVIOUS experiments¹ with lenses cultured in vitro with labeled glycine have shown that the tripeptide glutathione turns over continuously, being degraded into its component amino acids and resynthesized at similar rates. A significant amount of labeled glycine in these experiments was also found in the lens proteins. The present study is concerned with whether the lens proteins are similarly in a state of flux and whether interconversions of amino acids occur in the lens.

No previous studies of the interconversions of amino acids and the turnover of lens proteins have been made, nor had a detailed analysis of the amino acid composition of lens proteins been reported at the time these studies were performed.² There has been a recent investigation, however, on the oxidative metabolism of amino acids. De Vincentiis and Auricchio³ demonstrated the ability of the lens to oxidize several amino acids to keto acids, which, . . . [Full Text PDF of this Article]

Author Affiliations
BOSTON

From the Howe Laboratory of Ophthalmology, Harvard Medical School.

Footnotes
This work was supported in part by a grant from the United States Atomic Energy Commission.

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