Changes in oxidation-reduction potential of cytochrome b observed in the presence of antimycin A.
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Three forms of a thiol proteinase inhibitor were isolated from rat liver cytosol. The monomeric inhibitor (pI 5.2) (TPI-1) formed a complex with cathepsin H even in the absence of reducing agents. The inhibitor with pI 5.0 (TPI-2) was inactive in the absence of reducing agents but was converted to an active inhibitor on addition of reducing agents such as dithiothreitol, GSH, cysteine, or 2-mercaptoethanol. The dimeric inhibitor (TPI-D) with an intermolecular disulfide bridge was also inactive and was converted to the active monomeric inhibitor on addition of dithiothreitol. TPI-2 is most likely a mixed disulfide with glutathione. One (Cys-3) of two cysteine residues exposed on the surface of the molecule of TPI-2 is involved in the formation of a mixed disulfide, and the other cysteine residue (Cys-64) is buried in the molecule. The activity of rat liver thiol proteinase inhibitor may possibly be regulated by formation of a protein mixed disulfide or by reduction of the mixed disulfide.
Dehydrogenases of glycolysis, Krebs' cycle and pentose phosphate shunt were investigated in the intestinal stages of T. gondii. The "oval stages" appeared to display the activity of all the enzymes studied differing in this from merozoites and macrogametocytes. The macrogametocytes displayed very low, if any, activity of the enzymes studied, even the mature parasites. Immediately after fertilization, sharp shifts were observed in the oxidative metabolism of the zygote: from very low or negative it became moderate to strong. This may be suggestive of the changes in metabolic requirements of the zygote which is no longer an intracellular parasite. In this respect macrogametocytes and zygotes of Toxoplasma resemble the corresponding stages of chicken and rabbit intestinal coccidia of the genus Eimeria.
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