<script type="text/javascript">
<!--
document.write('<div id="oa_widget"></div>');
document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=undefined&type=result"></script>');
-->
</script>
Gliadin and glutenin were treated with various concentrations of 2-mercaptoethanol (ME) at pH 6.0 and their effects on protein disulfides were investigated. The treatment caused polymerization of gliadin, demonstrating the involvement of its disulfides in SH-SS exchange reaction. A plot of SH liberation of protein against ME concentration revealed the existence of a group of glutenin disulfides which reacted rapidly and quantitatively even in the low concentrations of ME, where reaction of the other disulfides was very slow. Most of gliadin disulfides were slowly reacting disulfides.
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 2 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |