Partial characterization of a minor chlorophyll-protein found in primary thylakoids of intermittently illuminated maize

Éva Sárvári, Gábor Gigler

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A mild solubilization with sodium dodecyl sulphate of intermittently illuminated maize (Zea mays L. Mvsc 429) thylakoids allows the separation of a minor chlorophyll-protein in the position of the light harvesting chlorophyll-protein monomer of green plants by polyacrylamide gel electrophoresis. It contains mainly chlorophyll a, its chlorophyll b content may come from the slightly contaminating light harvesting chlorophyll a/b-protein. It represents about 15% of the chlorophyll in protochloroplasts. The new chlorophyll-protein has an absorption maximum at 672 nm, and only one fluorescence emission peak at 680 nm. A 34 kD polypeptide is the most abundant one in the polypeptide pattern of the complex. The function of the new chlorophyll-protein is unknown at present. Its relationship to other chlorophyll-proteins is discussed.

Original languageEnglish
Pages (from-to)159-167
Number of pages9
JournalPhotosynthesis research
Volume5
Issue number2
DOIs
Publication statusPublished - Jun 1 1984

Keywords

  • Chlorophyll-protein
  • intermittent illumination
  • maize
  • primary thylakoid

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology

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