The mechanism of inactivation of rabbit liver phosphorylase phosphatase by glutathione disulfide (GSSG) was investigated. The catalytic subunit of phosphorylase phosphatase was inactivated by GSSG and other disulfides. Inactivation by GSSG was a concentration-dependent process and resulted in the formation of an inactive, stable enzyme species. The inactivated enzyme could be reactivated by add...

A subunit structure for human superoxide dismutase has been demonstrated by sedimentation equilibrium, agarose gel filtration, and sodium dodecyl sulfate polyacrylamide gel electrophoretic studies. This protein appears to be composed of 2 subunits, not linked by covalent bonds, each with a molecular weight about 16,000. Dissociation of the subunits is facilitated by alkylation of the two sulfhy...

The binding of mercury to red blood cells was measured in terms of Hg(203) uptake and desorption. The significant features of the binding are: (a) rapid achievement of equilibrium (3 to 5 minutes); (b) release of a Hg-complexing material from the red cells themselves which distorts the binding curves at low concentrations of metal (2.5 x 10(-7) to 5.0 x 10(-6)M); (c) prevention of binding by cy...

Cereal Chem. 72(l):58-64 A dynamic rheometer was used to characterize the effect of glutathione, interchange. Addition of potassium bromate to dough resulted an increase potassium bromate, and two ascorbic acid isomers on the rheological in G'and a decrease in loss tangent. L-threoascorbic acid was rheologically properties of wheat flour doughs. During resting after mixing (dough more effective...