Model studies regarding the internal corrosion of tin-plated food cans. III. Binding of tin(II) ions and iron(II) ions by sulfur-containing amino acids

1973 ◽  
Vol 21 (2) ◽  
pp. 246-251 ◽  
Author(s):  
Dieter W. Gruenwedel ◽  
Hsien-Chung Hao
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).


2016 ◽  
Vol 14 (44) ◽  
pp. 10473-10480 ◽  
Author(s):  
Sylvain Daunay ◽  
Remi Lebel ◽  
Laurence Farescour ◽  
Jean-Claude Yadan ◽  
Irene Erdelmeier

Natural and novel sulfur-containing amino acids are preparedviaa new regioselective one-pot two-step procedure.


2006 ◽  
Vol 26 (8) ◽  
pp. 3149-3163 ◽  
Author(s):  
Christophe Leroy ◽  
Laëtitia Cormier ◽  
Laurent Kuras

ABSTRACT Mediator is a key RNA polymerase II (Pol II) cofactor in the regulation of eukaryotic gene expression. It is believed to function as a coactivator linking gene-specific activators to the basal Pol II initiation machinery. In support of this model, we provide evidence that Mediator serves in vivo as a coactivator for the yeast activator Met4, which controls the gene network responsible for the biosynthesis of sulfur-containing amino acids and S-adenosylmethionine. In addition, we show that SAGA (Spt-Ada-Gcn5-acetyltransferase) is also recruited to Met4 target promoters, where it participates in the recruitment of Pol II by a mechanism involving histone acetylation. Interestingly, we find that SAGA is not required for Mediator recruitment by Met4 and vice versa. Our results provide a novel example of functional interplay between Mediator and coactivators involved in histone modification.


1981 ◽  
Vol 36 (3) ◽  
pp. 370-374 ◽  
Author(s):  
Shinji Ohmori ◽  
Kazuko Takahashi ◽  
Mikiko Ikeda ◽  
Toshihiko Ubuka

Abstract The desulfurization of several naturally occurring sulfur-containing amino acids by Raney nickel was studied under various conditions. Raney nickel, which was prepared by treating Al-Ni alloy with 5 N NaOH at 60 °C for 30 min, and was not washed with water, was most active and desulfurized, in quantitative yield, methionine, homocysteine, homocystine, homocysteine sulfinic acid, S-(2-carboxy-n-propyl)-L-cysteine, cysteine, cystine, cysteine sulfinic acid and S-methylcysteine sulfoxide. Raney nickel prepared from 100 mg of Al-Ni alloy desulfurized quantitatively up to 40 μmol methionine at 60 °C for 30 min. The desulfurization occurred effectively in the pH range of 7 and 13, but not below 7. Methionine sulfone, cysteic acid, and homocysteic acid were not subject to the reaction. The Raney nickel was deactivated by H2S, and H2O2, or combustion. Desulfurization activity was not enhanced by hydrogen gas.


Sign in / Sign up

Export Citation Format

Share Document