Publisher Summary Glutathione (GSH) is the most important nonprotein thiol in living systems and is of widespread occurrence in the intracellular milieu of animals, plants, and microorganisms GSH was isolated and named by the English biochemist Frederick Gowland Hopkins This chapter discusses 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 GSH-related biochemical reactions and the biological roles of GSH are discussed in the chapter The use of perturbations in GSH status as a means for investigating GSH-related phenomena and an analysis of the consequences of perturbation are presented A short summary of genetic lesions related to GSH is also included Like chemically induced perturbations in GSH status, genetic lesions provide valuable insights into the role of GSH in normal functions and processes in cells The chapter concludes with some brief comments about the future of the relationship of GSH status to cellular processes

The Glutathione Status of Cells

Publisher Summary The process of thiol/disulfide exchange provides a mechanism for the equilibration of the sulfhydryl oxidation state of proteins with the thiol/ disulfide status of the surrounding environment. If this process occurs in vivo and results in changes in the activities of certain enzymes, changes in enzyme activity could be coupled to changes in the redox potential of the cell. This chapter examines the possibility of metabolic regulation by thiol/disulfide exchange with respect to each of the six criteria: (1) the intracellular thiol/disulfide status should vary in vivo in response to some metabolic signal; (2) the oxidation of protein sulfhydryl groups by thiol/disulfide exchange should activate some enzymes, inactivate others, and not affect the activities of others; (3) the thiol/disulfide redox potential of a regulated protein should be near the observed thiol/disulfide ratio in vivo ; (4) thiol/disulfide exchange reactions must be kinetically competent under physiological conditions; (5) for regulated enzymes, the oxidized and reduced forms of the enzyme should both be observable in vivo ; and (6) the response of particular enzyme activities to oxidation by thiol/ disulfide exchange should be consistent with the metabolic function of the enzyme.

Redox control of enzyme activities by thiol/disulfide exchange.

Lipid peroxidation: A possible mechanism of cephaloridine-induced nephrotoxicity

Further evidence of molecular alteration and aberration of erythrocyte pyruvate kinase

Erythrocyte pyruvate kinase (PK) from 5 patients with congenital non-spherocytic hemolytic anemia and erythrocyte PK deficiency have been studied by immunological methods and electrofocusing.

J.K. Kruyta

Papers

On the molecular basis of pyruvate kinase deficiency. I. Primary defect or conseqence of increased glutathione disulfide concentration.