ArticlePolymers2020
Does Subunit Composition Influence the Intermolecular Crosslinking of Fish Collagen? A Study with Hake and Blue Shark Skin Collagens.
Article in Polymers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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
8 citing papers in PubMed.
- Ionogels Derived from Fluorinated Ionic Liquids to Enhance Aqueous Drug Solubility for Local Drug Administration.Gels (Basel, Switzerland) · 2022Article
- Article
- Molecular Weight Analysis of Blue Shark (International journal of molecular sciences · 2021Article
- Extraction and Characterization of Gelatin from Skin By-Products of Seabream, Seabass and Rainbow Trout Reared in Aquaculture.International journal of molecular sciences · 2021Article
- Production and Physicochemical Characterization of Gelatin and Collagen Hydrolysates from Turbot Skin Waste Generated by Aquaculture Activities.Marine drugs · 2021Article
- Characterization of Gelatin and Hydrolysates from Valorization of Farmed Salmon Skin By-Products.Polymers · 2021Article
- Sea Cucumber Derived Type I Collagen: A Comprehensive Review.Marine drugs · 2020Review
- Application of marine collagen for stem-cell-based therapy and tissue regeneration (Review).Medicine internationalReview
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Acid-soluble collagens from European hake and Blue shark skin were isolated, characterized, and compared. As the structure of collagen determines its function, the final objective of this study was to investigate biochemical differences between both collagens to identify future potential applications. Chromatographic behavior revealed differences in collagen from both species. Increases of temperature and stirring time produced no effect on European hake collagen solubility in the mobile phase, resulting in the same chromatographic profiles. Conversely, the application of temperature and stirring-time increments showed a positive effect on Blue shark collagen solubility, resulting in different chromatographic profiles and observing higher molecular weight components when sample is incubated at 50 °C (15 min) after 48 h stirring. To test if the different chromatographic behavior exhibited by both collagens could be influenced by differences in subunit composition (alpha-chains), cation exchange chromatography was employed to separate collagen subunits. The electrophoretic patterns and gel permeation chromatography with light-scattering detection (GPC-LS) results of the obtained cation exchange peak fractions revealed differences regarding subunit composition between both species, influencing the crosslinking pattern. This is the first comparative study using GPC-LS to provide information of European hake and Blue shark collagen subunit composition.
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