Paolo Cerletti

TL;DR: The seed globulins of Lupinus albus were extracted and 12 ditterent proteins were separated: four of them correspond to vicilins and two to legumin.

TL;DR: A biologically active spinach ferredoxin was reconstituted from the apoprotein by incubation with catalytic amounts of the sulfurtransferase rhodanese in the presence of thiosulfate, reduced lipoate and ferric ammonium citrate.

TL;DR: The interaction of the sulfurtransferase rhodanese with succinate dehydrogenase greatly decreases the catalytic activity of rhodAnese with respect to thiocyanate formation and there is an effect of the sulphurtransferase on the iron-sulfur absorption of the flavorprotein.

TL;DR: In this article, the intrinsic fluorescence, the fluorescence developed on titration with 8-aniline-1-naphthalene sulfonate (ANS), the UV spectra with second derivatives and solution stability were measured on acetic acid extracts of the glutens.

TL;DR: In this paper, it was shown that rhodanese-sulfur cluster formation is one of the functions of rhodanoese and showed that the enzyme seems to facilitate the build up of the cluster of spinach apoferredoxin.