ArticleJournal of protein chemistry2002
Effect of chaotropic agents on the structure-function of recombinant acylpeptide hydrolase.
Article in Journal of protein chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Chaotropic Agent-Assisted Supported Lipid Bilayer Formation.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Proteomics Methodologies: The Search of Protein Biomarkers Using Microfluidic Systems Coupled to Mass Spectrometry.Proteomes · 2023Review
- Functional Expression and Characterization of the Recombinant N-Acetyl-Glucosamine/N-Acetyl-Galactosamine-Specific Marine Algal Lectin BPL3.Marine drugs · 2018Article
- Identification and characterisation of a novel acylpeptide hydrolase from Sulfolobus solfataricus: structural and functional insights.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Acylpeptide hydrolase, a new class the serine-type peptidase, belongs to the alpha,beta hydrolase group of proteins. The tetrameric enzyme showed varying degree of stability in the presence of 1-8 M urea. The enzyme displayed about 15% of its original activity when treated with 8 M urea for 1 h at 25 degrees C. Complete recovery of the enzyme activity was observed on dialysis or dilution (50-fold) of the denatured enzyme. However, complete abolition of the enzyme activity was observed in the presence of 1 M GnHCl. Dialysis of the 1 M GnHCl-treated enzyme resulted in 15-20% recovery of the enzyme activity. The fluorescence emission spectra of the native enzyme at 337 nm showed a red shift up to 16 nm in 8 M urea and 18 nm in the presence of 4 M GnHCl. Native enzyme during far-UV circular dichroism spectroscopy exhibited predominantly beta-sheet structure. The enzyme lost its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure was minimally perturbed below 4 M urea. However, in 1 M GnHCl the enzyme lost both its secondary and tertiary structures and the enzyme was found to dissociate into monomers of 70 kDa. Both monomeric and dimeric species were observed after 24-h dialysis of the enzyme denatured with GnHCl indicating the reassociation process. Both monomer and dimers forms recovered after dialysis were active.
Indexed as
Identifiers
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Registered trials
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