TY - JOUR
T1 - High molecular weight pea leaf protein similar to the groE protein of escherichia coli
AU - Pushkin, Alexander V.
AU - Tsuprun, Vladimir L.
AU - Solovjeva, Nadejda A.
AU - Shubin, Vladimir V.
AU - Evstigneeva, Zinaida G.
AU - Kretovich, Waclaw L.
PY - 1982/6/4
Y1 - 1982/6/4
N2 - 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.
AB - 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.
KW - (Pea leaf)
KW - Electron microscopy
KW - High molecular weight protein
KW - groE gene
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U2 - 10.1016/0167-4838(82)90169-8
DO - 10.1016/0167-4838(82)90169-8
M3 - Article
AN - SCOPUS:0019915089
SN - 0167-4838
VL - 704
SP - 379
EP - 384
JO - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
JF - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
IS - 2
ER -