Polypeptide composition of a Photosystem II core complex. Presence of a herbicide-binding protein

K. Satoh, H. Y. Nakatani, K. E. Steinback, J. Watson, C. J. Arntzen

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110 Scopus citations


The polypeptide composition of a Photosystem II (PS II) core complex from higher plant chloroplasts has been characterized by subjecting the isolated complex to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two polypeptides in the 40-50 kDa size class, attributed to the chlorophyll a-binding apoproteins of PS II, were resolved when the urea concentration in the SDS-polyacrylamide gel electrophoresis was greater than 1 M. The two chlorophyll a-binding proteins were dissimilar in their primary structure based upon their different hydrolysis products on SDS-polyacrylamide gel electrophoresis following papain treatment. The core complex contained three additional polypeptides. Two polypeptides in the 30-34 kDa size class were resolved when the urea concentration in the gel system was increased to greater than 4 M. One of the polypeptides in this size class was identified as the herbicide-binding protein from azido[14C]atrazine labeling studies. The herbicide-binding protein displayed an anomalous electrophoretic migration behavior in SDS-polyacrylamide gel electrophoresis in the presence or absence of urea; its apparent molecular weight decreased when the urea concentration increased. The fifth protein component of the core complex was attributed to cytochrome b-559 which was found to consist of the ascorbate- and dithionite-reducible forms in the samples prior to SDS solubilization.

Original languageEnglish (US)
Pages (from-to)142-150
Number of pages9
JournalBBA - Bioenergetics
Issue number1
StatePublished - Jul 29 1983


  • Atrazine
  • Chlorophyll fluorescence
  • Herbicide-binding protein
  • Photosystem II
  • Polypeptide composition

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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