High molecular weight pea leaf protein similar to the groE protein of escherichia coli

Alexander V. Pushkin, Vladimir L. Tsuprun, Nadejda A. Solovjeva, Vladimir V. Shubin, Zinaida G. Evstigneeva, Waclaw L. Kretovich

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Abstract

A high molecular weight protein which in its structure and some properties is similar to the groE protein of Escherichia coli, has been found in pea leaves. Using electron microscopy we established that the protein consisted of 14 identical monomers which are arranged with point 72 symmetry in two layers, seven monomers in each layer. The molecular weight of the protein, determined by gel filtration and sedimentation equilibrium techniques, was found to be 900000 ∓ 150000 and 950000 ∓ 50000, respectively. The sedimentation coefficient was 24.3 ∓ 1.0S. During polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the protein dissociated into identical polypeptide chains of Mr 67000 ∓ 3000. On the basis of the circular dichroism spectrmn file share of α-helical portions was found to be 0.47∓0.06, that of β-structures 0.13∓0.03, that of β-turn 0.16∓0.03, and that of irregular portions 0.24∓0.07. The protein had a low ATPase (EC 3.6.1.3) activity. The protein content in the leaves was found to vary with their growth stage.

Original languageEnglish (US)
Pages (from-to)379-384
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume704
Issue number2
DOIs
StatePublished - Jun 4 1982

Keywords

  • (Pea leaf)
  • Electron microscopy
  • High molecular weight protein
  • groE gene

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