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JIN H. KINOSHITA, Ph.D.; THOMAS MASURAT, B.A.

AMA Arch Ophthalmol. 1957;57(2):266-274.

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

Introduction

Many investigators have reported on the presence of glutathione (GSH) in lens.¹ Glutathione has been suspected of serving some important functions in the physiology of the lens, since one of the first observable changes in experimental cataract formation is a marked decrease in GSH concentration. The reason for the presence of the unusually high concentrations of GSH has never been adequately explained. It has been definitely established that one of the factors contributing to the presence of this tripeptide is that the lens is capable of its synthesis. The incorporation of radioactive glycine into the glutathione molecule was demonstrated to occur in the lens by Kinsey and Merriam.² Recently, GSH synthesis from its component amino acids in lens homogenates was observed by Daisley.³

However, other factors leading to the accumulation of this tripeptide have not been thoroughly studied. The present paper is an attempt in this . . . [Full Text PDF of this Article]

Author Affiliations
Boston

From the Howe Laboratory of Ophthalmology Harvard Medical School and Massachusetts Eye and Ear Infirmary.

Footnotes
Received for publication Sept. 4, 1956.

This project was supported by the Atomic Energy Commission.

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