Relationship between reductase and thiol oxidase activities and the content of low molecular thiols in developing seeds of spring wheat
1993
Trufanov, V.A. | Permyakov, A.V. | Kichatinova, S.V.
Four genotypically different forms of spring soft wheat were used to study changes in the content of low molecular SH-compounds with the activity of thiol:protein-disulfide oxidoreductase (EC 1.8.4.2) and thiol:oxygen oxidoreductase (EC 1.8.3.2) catalyzing the reactions of thiol-disulfide metabolism in developing wheat seeds. During intensive biosynthetic processes associated with maturation of seeds, the specific disulfide reductase activity correlated directly with the content of nonprotein SH-groups, which in turn may be determined by the activity of oxyden-dependent thiol oxidase, highly specific to low molecular SH-compounds. It is suggested that nonprotein SH-groups, in particular reduced glutathione, may be involved in regulation of the activity of the enzymes responsible for thiol-disulfide balance at different stages of wheat seed maturation
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