The present article discusses the concept of synderesis in the late medieval universities of Erfurt and Leipzig and its the later developments in Wittenberg. The comparison between Bartholomaeus Arnoldi of Usingen in Erfurt and Johannes Peyligk in Leipzig shows that school traditions played an important role in the exposition of synderesis by the late medieval scholastic natural philosophers. However, Jodocus Trutfetter's example warns against overemphasising the importance of the school traditions and reminds us of the manifold history of medieval discussions on synderesis, which were more or less familiar to many authors of this period. Finally, the diverse references to synderesis in the texts of Martin Luther, Johannes Bernhardi of Feldkirch and Philip Melanchthon reveal no uniform relationship with late medieval discussions, but rather indicate various ways of adopting scholastic ideas and transforming them in the context of humanist and reformation thinking.

Proteins in the thioredoxin superfamily share a similar fold, contain a -CXXC- active site, and catalyze oxidoreductase reactions by dithiol-disulfide exchange mechanisms. Protein disulfide isomerase (PDI) has two -CGHC- active sites. For in vitro studies, oxidation/reduction of PDI during the catalytic cycle is accomplished with glutathione. Glutathione may act as electron donor/acceptor for PDI also in vivo, but at least for oxidation reactions, GSSG probably is not the major electron acceptor and PDI may not have evolved to react with glutathione with high affinity, but merely having adequate affinity for both glutathione and folding proteins/peptides. Glutaredoxins, on the other hand, have a high affinity for glutathione. They commonly have -CXFC- or -CXYC- active site, where the tyrosine residue forms part of the GSH binding groove. Mutating the active site of PDI to a more glutaredoxin-like motif increased its reactivity with glutathione. All such variants showed an increased rate in GSH-dependent reduction or GSSG-dependent oxidation of the active site, as well as a decreased rate of the native disulfide bond formation, with the magnitude of the effect increasing with glutathione concentration. This suggests that these variants lead to competition in binding between glutathione and folding protein substrates.

In 1513 the Fifth Lateran Council determined that the immortality of the rational soul is not true only in theology, but also in philosophy. The determination can be related also to the actual teaching of philosophy. In the university of Erfurt, Bartholomaeus Arnoldi de Usingen and Jodocus Trutfetter wrote expositions on natural philosophy at that time. Usingen's and Trutfetter's expositions of De anima represent a position, which faithfully follows in methodology and aspirations the tradition of the via moderna. Furthermore, they give an interpretation of the relationship between philosophy and theology, which Trutfetter considered consonant with the intentions and the formulations of the Fifth Lateran Council; and finally, Trutfetter even presents a practical application of the Council's recommendations.

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