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Open AccessJournal ArticleDOI

Free and protein-bound glutathione in normal and cataractous human lenses.

John J. Harding
- 01 May 1970 - 
- Vol. 117, Iss: 5, pp 957-960
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TLDR
Study of normal and cataractous human lenses showed that their glutathione content is age-dependent, decreasing steadily from about 3.5mumol/g of lens at age 20 years to about 1.8mumols/g at age 65 years.
Abstract
Protein-bound glutathione was identified and measured in normal and cataractous human lenses. In a major group of cataracto us lenses the bound glutathione concentration was higher than normal. Study of normal lenses showed that their glutathione content is age-dependent, decreasing steadily from about 3.5mumol/g of lens at age 20 years to about 1.8mumol/g of lens at age 65 years. Cataract brings further decreases.

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Book ChapterDOI

The Glutathione Status of Cells

TL;DR: GSH status, the biologically relevant chemistry of GSH, the forms in which GSH can be present within the cell, along with the GSH content of cells and the methods for analysis of this substance are discussed.
Journal ArticleDOI

Glutathione dysregulation and the etiology and progression of human diseases.

TL;DR: The present report highlights and integrates the growing connections between imbalances in GSH homeostasis and a multitude of human diseases and suggests the high GSH content makes cancer cells chemoresistant, which is a major factor that limits drug treatment.
Journal ArticleDOI

Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death.

TL;DR: A GSH-depletion model of neurodegenerative disorders is provided, experimental verifications of this model are suggested, and potential therapeutic approaches for preventing or halting these diseases are proposed.
References
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Journal ArticleDOI

Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent

TL;DR: A simple spectrophotometric method for the routine concomitant determination of sulfhydryl groups in PB- SH, NP-SH, and T-SH fractions in various tissues is reported.
Journal ArticleDOI

Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

Brown, +1 more
- 01 Oct 1966 - 
TL;DR: By applying this method to bovine chymotrypsinogen A, it was found that the half-cystine residues were linked 1-122, 42-58, 136-201, 168-182 and 191-220, which reveals the way in which the cysteic acid peptides were originally joined in the protein.
Journal ArticleDOI

Cellular mixed disulphides between thiols and proteins, and their possible implication for radiation protection.

TL;DR: It is suggested that protein bound glutathione may represent a reservoir of physiological radiation protector and be of significance or the radio protective action of cysteamine.