ArticlePloS one2015
Comprehensive Analysis of a Vibrio parahaemolyticus Strain Extracellular Serine Protease VpSP37.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
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- Isolation and enzyme bioprospection of bacteria associated toBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Neural Crest-Derived Chondrocytes Isolation for Tissue Engineering in Regenerative Medicine.Cells · 2020Article
- Quorum-Sensing Regulator OpaR Directly Represses Seven Protease Genes inFrontiers in microbiology · 2020Article
- A GntR Family Transcription Factor (VPA1701) for Swarming Motility and Colonization ofPathogens (Basel, Switzerland) · 2019Article
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- A modified culture medium for improved isolation of marine vibrios.MicrobiologyOpen · 2019Article
- A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light onInternational journal of molecular sciences · 2019Article
- The Anemonia viridis Venom: Coupling Biochemical Purification and RNA-Seq for Translational Research.Marine drugs · 2018Review
- The extracellular proteases produced by Vibrio parahaemolyticus.World journal of microbiology & biotechnology · 2018Review
- Article
- Metallothionein Gene Family in the Sea Urchin Paracentrotus lividus: Gene Structure, Differential Expression and Phylogenetic Analysis.International journal of molecular sciences · 2017Article
- Maintenance of a Protein Structure in the Dynamic Evolution of TIMPs over 600 Million Years.Genome biology and evolution · 2016Article
- A Zinc-Dependent Protease AMZ-tk from a Thermophilic Archaeon is a New Member of the Archaemetzincin Protein Family.Frontiers in microbiology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain between residues 35 and 276 and a canonical Trypsin/Chimotrypsin 3D structure. Functional assays were performed to evaluate protease activity of purified enzyme. Additionally the performance of VpSP37 was evaluated in tissue dissociations experiments and the use of such enzyme as a component of enzyme blend for tissue dissociation procedures is strongly recommended.
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