ArticleJournal of conservative dentistry and endodontics2025
Standardization of extraction, identification, and characterization of an immunoglobulin Y antibody: A potential inhibitor of cariogenic and endodontic microbiome.
Article in Journal of conservative dentistry and endodontics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Formation and preliminary characterization of mercury-reactive immunoglobulin Y antibodies in laying hens using HgClVeterinary world · 2026Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aim: This study aimed to formulate a protocol to isolate and characterize immunoglobulin Y (IgY) antibodies from chicken egg yolk and evaluate its potential in inhibiting Materials and Methods: Part A: IgY was extracted from fresh chicken egg yolk using a polyethylene glycol precipitation method. The isolated IgY was characterized using ultraviolet-visible (UV-Vis) spectroscopy to assess protein concentration and purity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight confirmation, high-performance liquid chromatography (HPLC) for purity, and mass spectrometry for further protein analysis. Functional activity was evaluated using Western blotting and enzyme-linked immunosorbent assay (ELISA) to confirm antigen binding. PART B: antimicrobial testing: (i) minimum inhibitory concentration (MIC) assays: determining the lowest concentration of IgY that inhibits the growth of each pathogen and (ii) zone of inhibition tests: measuring the effectiveness of IgY in inhibiting pathogen growth on agar plates. The concentration of IgY 50 μl, and 100 μl was utilized against Results: The UV-Vis spectroscopy results indicated a high concentration of IgY with minimal impurities. SDS-PAGE revealed a single band at approximately 180 kDa, corresponding to the expected molecular weight of IgY, with no significant contamination. HPLC analysis confirmed a pure IgY preparation with a single major peak. Mass spectrometry further validated the molecular weight of the IgY at ~180 kDa. Functional assays (western blotting and ELISA) demonstrated that the isolated IgY retained its ability to bind specifically to Conclusion: IgY antibodies isolated from chicken egg yolk were characterized as highly pure and functional, with a strong potential for use in inhibiting
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