Orientation of plgments in the thylakoid membrane and in the isolated chlorophyll-protein complexes of higher plants. IV. The 100 K linear dichroism spectra of thylakoids from wild-type and chlorophyll b-less barley thylakoids

Philip Haworth, Pierre Tapie, C. J. Arntzen, Jacques Breton

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Using a polyacrylamide gel squeezing technique, linear dichroism spectra of thylakoids from wild-type and chlorophyll-b less barley have been obtained at 100 K. The calculated difference linear dichroism spectra, based on normalization at 690-695 nm, are identical to those of the light-harvesting complex (LHC) isolated by Triton solubilization. This observation is in agreement with previous conclusions (Tapie, P., Haworth, P., Hervo, G. and Breton, J. (1982) Biochim. Biophys. Acta 682, 339-344) regarding: (i) scattering artifacts are absent in linear dichroism spectra determined using polyacrylamide gels, (ii) the in vivo orientation of LHC pigments is maintained in the isolated complex and (iii) the largest dimension(s) of the isolated LHC is (are), in vivo, parallel to the plane of the photosynthetic membrane.

Original languageEnglish (US)
Pages (from-to)504-506
Number of pages3
JournalBBA - Bioenergetics
Issue number3
StatePublished - Dec 15 1982



  • (Barley chloroplast)
  • Chlorophyll-protein complex
  • Linear dichroism
  • Thylaloid membrane

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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