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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
1983-12-20
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pubmed:abstractText |
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.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0320-9725
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1441-6
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6626605-Circular Dichroism,
pubmed-meshheading:6626605-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6626605-Fabaceae,
pubmed-meshheading:6626605-Macromolecular Substances,
pubmed-meshheading:6626605-Molecular Weight,
pubmed-meshheading:6626605-Plant Proteins,
pubmed-meshheading:6626605-Plants,
pubmed-meshheading:6626605-Plants, Medicinal,
pubmed-meshheading:6626605-Protein Conformation
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pubmed:year |
1983
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pubmed:articleTitle |
[High molecular weight protein consisting of 14 monomers from pea leaves].
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pubmed:publicationType |
Journal Article,
English Abstract
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