ArticleThe journal of venomous animals and toxins including tropical diseases2019
Proteome of fraction from
Article in The journal of venomous animals and toxins including tropical diseases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
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- Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom.Toxins · 2024Article
- Mass spectrometric analysis of Odonthobuthus Doriae scorpion venom and its non-neutralized fractions after interaction with commercial antivenom.Scientific reports · 2024Article
- Understanding the complexity ofThe journal of venomous animals and toxins including tropical diseases · 2024Review
- Identification of an Antimicrobial Peptide from the Venom of the Trinidad Thick-Tailed ScorpionAntibiotics (Basel, Switzerland) · 2023Article
- BotCl, the First Chlorotoxin-like Peptide Inhibiting Newcastle Disease Virus: The Emergence of a New Scorpion Venom AMPs Family.Molecules (Basel, Switzerland) · 2023Article
- Toxinology in the proteomics era: a review on arachnid venom proteomics.The journal of venomous animals and toxins including tropical diseases · 2022Article
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- Self-Assembled Cationic-Covered Nanoemulsion as A Novel Biocompatible Immunoadjuvant for Antiserum Production AgainstPharmaceutics · 2020Article
- Investigation of the structure-activity relationship in ponericin L1 fromPeptide science (Hoboken, N.J.) · 2020Article
- Natural Occurrence in Venomous Arthropods of Antimicrobial Peptides Active against Protozoan Parasites.Toxins · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
background
methodsFraction I was obtained by a cation exchange chromatography using 50 mg of crude venom. This fraction was subjected to a biochemical characterization, including determination of L-amino acid oxidase, phospholipase, hyaluronidase, proteases activities and inhibition of angiotensin converting enzyme (ACE) activity. Fraction I was submitted to reduction, alkylation and digestion processes, and the tryptic digested peptides obtained were analyzed in a Q-Exactive Orbitrap mass spectrometer. Data analysis was performed by PEAKS 8.5 software against NCBI database.
resultsFraction I exhibits proteolytic activity and it was able to inhibit ACE activity. Its proteome analysis identified 8 different classes of venom components, among them: neurotoxins (48%), metalloproteinases (21%), hypotensive peptides (11%), cysteine-rich venom protein (9%), antimicrobial peptides (AMP), phospholipases and other enzymes (chymotrypsin and lysozymes) (3%) and phosphodiesterases (2%).
conclusionsThe combination of a proteomic and biochemical characterization strategies leads us to identify new components in the
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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.