ArticlePloS one2014
Extremely stable soluble high molecular mass multi-protein complex with DNase activity in human placental tissue.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- DNase Activities of a Highly Stable High-Molecular-Mass Multiprotein Complex Isolated from Different Organs of the Sea CucumberInternational journal of molecular sciences · 2026Article
- Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix.The protein journal · 2026Article
- Phosphatase Activities of a Highly Stable High-Molecular-Mass Multiprotein Complex Isolated from Different Organs of the Sea CucumberInternational journal of molecular sciences · 2026Article
- Stable and Specific Multiprotein Complexes with High Molecular Masses in Different Organs of the Sea CucumberInternational journal of molecular sciences · 2026Article
- Very Stable High-Molecular-Mass Multiprotein Complexes in Different Organs of the Sea CucumberMolecules (Basel, Switzerland) · 2025Article
- Analysis of Proteins and Peptides of Highly Purified CD9International journal of molecular sciences · 2022Article
- Protease and DNase Activities of a Very Stable High-Molecular-Mass Multiprotein Complex from Sea CucumberInternational journal of molecular sciences · 2022Article
- Comparison of the Content of Several Elements in Seawater, Sea CucumberMolecules (Basel, Switzerland) · 2022Article
- Very Stable Two Mega Dalton High-Molecular-Mass Multiprotein Complex from Sea CucumberMolecules (Basel, Switzerland) · 2021Article
- Immunosuppressive Effects of Mesenchymal Stem Cells-derived Exosomes.Stem cell reviews and reports · 2021Review
- Extra Purified Exosomes from Human Placenta Contain An Unpredictable Small Number of Different Major Proteins.International journal of molecular sciences · 2019Article
- Comparison of Trace Elements in High-Molecular-Mass Multiprotein Complex and in Female Milk from Which It Was Obtained.TheScientificWorldJournal · 2019Article
- Purified horse milk exosomes contain an unpredictable small number of major proteins.Biochimie open · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human placenta is an organ which protects, feeds, and regulates the grooving of the embryo. Therefore, identification and characterization of placental components including proteins and their multi-protein complexes is an important step to understanding the placenta function. We have obtained and analyzed for the first time an extremely stable multi-protein complex (SPC, ∼ 1000 kDa) from the soluble fraction of three human placentas. By gel filtration on Sepharose-4B, the SPC was well separated from other proteins of the placenta extract. Light scattering measurements and gel filtration showed that the SPC is stable in the presence of NaCl, MgCl2, acetonitrile, guanidinium chloride, and Triton in high concentrations, but dissociates efficiently in the presence of 8 M urea, 50 mM EDTA, and 0.5 M NaCl. Such a stable complex is unlikely to be a casual associate of different proteins. According to SDS-PAGE and MALDI mass spectrometry data, this complex contains many major glycosylated proteins with low and moderate molecular masses (MMs) 4-14 kDa and several moderately abundant (79.3, 68.5, 52.8, and 27.2 kDa) as well as minor proteins with higher MMs. The SPC treatment with dithiothreitol led to a disappearance of some protein bands and revealed proteins with lower MMs. The SPCs from three placentas efficiently hydrolyzed plasmid supercoiled DNA with comparable rates and possess at least two DNA-binding sites with different affinities for a 12-mer oligonucleotide. Progress in study of placental protein complexes can promote understanding of their biological functions.
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