Abstract
A new high molecular weight protein has been detected in pea leaves. Using electron microscopy it has been demonstrated that this protein consists of 14 identical monomers with a point 72 symmetry arranged in two layers, 7 monomers in each. The molecular weight of the protein as determined by gel filtration and sedimentation equilibrium method is equal to 900000 +/- 150000 and 950000 +/- 50000, respectively. The sedimentation coefficient for the protein is 24.3 +/- 1.0S. During SDS polyacrylamide gel electrophoresis the protein dissociates into identical polypeptide chains with molecular weight of 67000 +/- 3000. The circular dichroism spectra of the protein reveal that the percentage of alpha-helix portions, beta-structures, beta-turns and irregular portions is 0.45 +/- 0.06, 0.31 +/- 0.03, 0.09 +/- 0.03 and 0.15 +/- 0.07, respectively. The protein possesses a weak ATPase activity. The protein content in the leaves changes in the course of development.
| Translated title of the contribution | High molecular weight protein consisting of 14 monomers from pea leaves |
|---|---|
| Original language | Russian |
| Pages (from-to) | 1441-1446 |
| Number of pages | 6 |
| Journal | Biokhimiya |
| Volume | 48 |
| Issue number | 9 |
| State | Published - Sep 1 1983 |