Investigation of gliadin binding to different selected proteins using a biotin-streptavidin system
Zeitschrift für Lebensmittel-Untersuchung und -Forschung, ISSN: 0044-3026, Vol: 198, Issue: 3, Page: 249-252
1994
- 10Citations
- 7Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations10
- Citation Indexes10
- 10
- CrossRef8
- Captures7
- Readers7
Article Description
Using a biotin streptavidin system 12 out of 19 different test proteins were found to bind to gliadin, with casein, fibrinogen, and fibronectin showing the strongest association. Binding was demonstrable using different gliadin subfractions and enzymatic digests. There was no consistent effect of several carbohydrates on binding. Binding of most proteins to gliadin was diminished slightly by removal of Ca and strongly by dioxane, ethylene glycol, Triton X-100, and Tween 20. The results suggest a non-selective association between gliadin and the proteins investigated, mainly due to hydrophobic interactions, which might be of significance in intestinal pathobiochemistry, e. g. disease. © 1994 Springer-Verlag.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028393823&origin=inward; http://dx.doi.org/10.1007/bf01192604; http://www.ncbi.nlm.nih.gov/pubmed/8178578; http://link.springer.com/10.1007/BF01192604; http://www.springerlink.com/index/10.1007/BF01192604; http://www.springerlink.com/index/pdf/10.1007/BF01192604; https://dx.doi.org/10.1007/bf01192604; https://link.springer.com/article/10.1007/BF01192604
Springer Science and Business Media LLC
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