On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts

B. Böddi, Agneta Lindsten, Margareta Ryberg, Christer Sundqvist

Research output: Contribution to journalArticle

118 Citations (Scopus)

Abstract

The inner membranes from wheat {Triticum aestivum L. cv. Walde) etioplasts were separated into membrane fractions representative of prolamellar bodies and prothylakoids by differential and gradient centrifugations. The isolated fractions were characterized by absorption-, low-temperature fluorescence-, and circular dichroism (CD) spectroscopy, by high performancy liquid chromatography and by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The prolamellar body fraction was enriched in NADPH-protochlorophyllide oxidoreductase (E.C. 1.6.99.1), and in protochlorophyllide showing an absorption maximum at 650 nm and a fluorescence emission maximum at 657 nm. Esterified protochlorophyllide was mainly found in the prothylakoid fraction. The carotenoid content was qualitatively the same in the two fractions. On a protein basis the carotenoid content was about three times higher in the prolamellar body fraction than in the prothylakoid fraction. The CD spectra of the membrane fractions showed a CD couplet with a positive band at 655 nm, a zero crossing at 643-644 nm and a negative band at 623-636 nm. These results differ from earlier CD measurements on protochlorophyllide holochrome preparations. The results support the interpretation that protochlorophyllide is present as large aggregates in combination with NADPH and NADPH-protochlorophyllide oxidoreductase in the prolamellar bodies.

Original languageEnglish
Pages (from-to)135-143
Number of pages9
JournalPhysiologia Plantarum
Volume76
Issue number2
DOIs
Publication statusPublished - 1989

Fingerprint

Protochlorophyllide
etioplasts
protochlorophyllides
protochlorophyllide reductase
Chloroplasts
Circular Dichroism
circular dichroism spectroscopy
Triticum
wheat
Carotenoids
NADP (coenzyme)
Membranes
Proteins
proteins
Fluorescence
oxidoreductases
carotenoids
Centrifugation
NADP
Liquid Chromatography

Keywords

  • Absorption spectra
  • Circular dichroism
  • Etioplasts
  • Fluorescence spectra
  • NADPH-protochlorophyllide oxidoreductase
  • Prolamellar bodies
  • Protochlorophyllide
  • Triticum aestivum
  • Wheat

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology
  • Genetics
  • Physiology

Cite this

On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts. / Böddi, B.; Lindsten, Agneta; Ryberg, Margareta; Sundqvist, Christer.

In: Physiologia Plantarum, Vol. 76, No. 2, 1989, p. 135-143.

Research output: Contribution to journalArticle

Böddi, B. ; Lindsten, Agneta ; Ryberg, Margareta ; Sundqvist, Christer. / On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts. In: Physiologia Plantarum. 1989 ; Vol. 76, No. 2. pp. 135-143.
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