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Photosynth Res. 1987 Jan;12(1):83-90. doi: 10.1007/BF00019153.

Fluorescence polarization of trypsin digested photosystem II membranes.

Photosynthesis research

R Paliwal, G S Singhal

Affiliations

  1. School of Life Sciences, Jawaharlal Nehru University, 110067, New Delhi, India.

PMID: 24435583 DOI: 10.1007/BF00019153

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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