chlorophyll-a has been researched along with sodium-sulfite* in 2 studies
2 other study(ies) available for chlorophyll-a and sodium-sulfite
Article | Year |
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Antiviral substance from silkworm faeces: characterization of its antiviral activity.
The antiviral activity of a substance (L4-1) purified from silkworm faeces was examined in an HVJ (Sendai virus)-LLC-MK2 cell system. Its antiviral effect depended on the period of light irradiation and was inhibited by sodium sulfite and anaerobic conditions. These results indicate that the antiviral activity of L4-1 is associated with active oxygen species produced from the substance. SDS-polyacrylamide gel electrophoretic analysis showed that viral proteins were damaged by this substance under light irradiation. The results suggest that the antiviral activity is due to damage to viral protein(s) caused by active oxygen species produced from L4-1. Topics: Animals; Antiviral Agents; Bombyx; Cell Line; Chlorophyll; Feces; Haplorhini; Light; Reactive Oxygen Species; Respirovirus; Sulfites; Viral Proteins | 2000 |
The effect of sulfite on the ATP hydrolysis and synthesis activity of membrane-bound H(+)-ATP synthase from various species.
The action of sulfite on ATP hydrolysis and synthesis activities is investigated in membrane vesicles prepared from the cyanobacterium Synechococcus 6716, chromatophores from the photosynthetic purple bacterium Rhodospirillum rubrum, membrane vesicles from the related non-photosynthetic bacterium Paracoccus denitrificans, and bovine heart submitochondrial particles. Without any further pretreatment ATP hydrolysis is stimulated by sulfite in all four membrane preparations. Typically ATP synthesis in the cyanobacterial membrane vesicles is inhibited by sulfite, whereas ATP synthesis in chromatophores and the submitochondrial particles is not. These differences in sensitivity of ATP synthesis to sulfite, however, correspond well with the distribution of (photosynthetic) sulfur oxidizing pathways in the remaining three organisms/organelles compared in this study. Topics: Adenosine Triphosphate; Animals; Bacterial Chromatophores; Cattle; Cell Membrane; Chlorophyll; Chlorophyll A; Cyanobacteria; Hydrolysis; Kinetics; Mitochondria, Heart; Paracoccus denitrificans; Proton-Translocating ATPases; Rhodospirillum rubrum; Submitochondrial Particles; Sulfites | 1994 |