Abstract
Fluorescence polarization of photosystem II particles treated with trypsin and incubated with high salt-medium (2M NaCl) was investigated. The presence of atrazine and TMPD in normal and salt-washed particles induced a decrease in the polarization ratios. Similar results were obtained at low concentrations of trypsin. On the basis of our observations we suggest that the presence of these perturbing agents causes a reorganisation of the membrane components and alters pigment-pigment and pigment-protein interactions. The results of fluorescence polarization demonstrate trypsin entry into the membrane after the digestion of the peripheral proteins.
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Abbreviations
- Chl:
-
chlorophyll
- Mes:
-
2-(N-morpholino)-ethanesulfonic acid
- OEC:
-
oxygen evolving complex
- PS II:
-
photosystem II
- TMPD:
-
N, N, N′
- N′:
-
tetramethyl-p-phenyl-enediamine
- DPH:
-
1, 6-diphenyl-1, 3, 5-hexatriene
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Paliwal, R., Singhal, G.S. Fluorescence polarization of trypsin digested photosystem II membranes. Photosynth Res 12, 83–90 (1987). https://doi.org/10.1007/BF00019153
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DOI: https://doi.org/10.1007/BF00019153