ArticleApplied and environmental microbiology2012
Enhancement of the structural stability of full-length clostridial collagenase by calcium ions.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
The trial behind it
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
10 citing papers in PubMed, 38 citations in OpenAlex.
- The mysterious case of missing lymphocytes: a cautionary tale of interinstitutional variability in outcomes of lung dissociation protocols.American journal of physiology. Lung cellular and molecular physiology · 2025Article
- Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024Review
- Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation.Biotechnology for biofuels and bioproducts · 2022Article
- Maturation Process and Characterization of a Novel Thermostable and Halotolerant Subtilisin-Like Protease with High Collagenolytic Activity but Low Gelatinolytic Activity.Applied and environmental microbiology · 2022Article
- Combinatorial approach for screening and assessment of multiple therapeutic enzymes from marine isolateRSC advances · 2019Article
- Characterization of the Kinetics and Mechanism of Degradation of Human Mesenchymal Stem Cell-Laden Poly(ethylene glycol) Hydrogels.ACS applied bio materials · 2019Article
- Article
- Collagen V Is a Potential Substrate for Clostridial Collagenase G in Pancreatic Islet Isolation.Journal of diabetes research · 2016Article
- Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.Journal of proteomics · 2014Article
- Solution structure of clostridial collagenase H and its calcium-dependent global conformation change.Biophysical journal · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The clostridial collagenases G and H are multidomain proteins. For collagen digestion, the domain arrangement is likely to play an important role in collagen binding and hydrolysis. In this study, the full-length collagenase H protein from Clostridium histolyticum was expressed in Escherichia coli and purified. The N-terminal amino acid of the purified protein was Ala31. The expressed protein showed enzymatic activity against azocoll as a substrate. To investigate the role of Ca(2+) in providing structural stability to the full-length collagenase H, biophysical measurements were conducted using the recombinant protein. Size exclusion chromatography revealed that the Ca(2+) chelation by EGTA induced interdomain conformational changes. Dynamic light scattering measurements showed an increase in the percent polydispersity as the Ca(2+) was chelated, suggesting an increase in protein flexibility. In addition to these conformational changes, differential scanning fluorimetry measurements revealed that the thermostability was decreased by Ca(2+) chelation, in comparison with the thermal melting point (T(m)). The melting point changed from 54 to 49°C by the Ca(2+) chelation, and it was restored to 54°C by the addition of excess Ca(2+). These results indicated that the interdomain flexibility and the domain arrangement of full-length collagenase H are reversibly regulated by Ca(2+).
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