ArticleProtoplasma2013
Biochemical characteristics of the Ca2+ pumping ATPase in the peribacteroid membrane from broad bean root nodules.
Article in Protoplasma, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 11 citations in OpenAlex.
- Nutrient-dependent regulation of symbiotic nitrogen fixation in legumes.Horticulture research · 2025Article
- Calcium in the Life Cycle of Legume Root Nodules.Indian journal of microbiology · 2023Review
- Transport processes of the legume symbiosome membrane.Frontiers in plant science · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ca(2+)-ATPase in the peribacteroid membrane (PBM) of symbiosomes isolated from Vicia faba root nodules was characterized in terms of its hydrolytic and transport activities. Both activities were found to be pH-dependent and exhibit pH optimum at pH 7.0. Translocation of Ca(2+) through the PBM by the Ca(2+)-ATPase was shown to be fueled by ATP and other nucleotide triphosphates in the following order: ATP > ITP ≅ GTP ≅ UTP ≅ CTP, the K m of the enzyme for MgATP being about 100 μM. Ca-dependent ITP-hydrolytic activity of symbiosomes was investigated in the presence of the Ca-EGTA buffer system and showed the affinity of PBM Ca(2+)-ATPase for Ca(2+) of about 0.1 μM. The transport activity of Ca(2+)-ATPase was inhibited by erythrosin B as well as orthovanadate, but markedly stimulated by calmodulin from bovine brain. These results allowed us to conclude that this enzyme belongs to IIB-type Ca(2+)-ATPases which are present in other plant membranes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.