Selective magnetic separation of sulfur-containing amino acids by sonochemically prepared Au/γ-Fe2O3 composite nanoparticles

2006 ◽  
Vol 54 (4) ◽  
pp. 609-613 ◽  
Author(s):  
Yoshiteru Mizukoshi ◽  
Satoshi Seino ◽  
Takuya Kinoshita ◽  
Takashi Nakagawa ◽  
Takao A. Yamamoto ◽  
...  
2005 ◽  
Vol 293 (1) ◽  
pp. 106-110 ◽  
Author(s):  
Takuya Kinoshita ◽  
Satoshi Seino ◽  
Yoshiteru Mizukoshi ◽  
Yohei Otome ◽  
Takashi Nakagawa ◽  
...  

2006 ◽  
Vol 05 (02n03) ◽  
pp. 359-363 ◽  
Author(s):  
YOSHITERU MIZUKOSHI ◽  
SATOSHI SEINO ◽  
KENJI OKITSU ◽  
TAKUYA KINOSHITA ◽  
TAKASHI NAKAGAWA ◽  
...  

We have successfully prepared Au nanoparticles by the sonochemically reducing Au(III) ions and immobilized them on the surface of magnetic γ- Fe 2 O 3 nanoparticles. Au particles with average diameter of about 10 nm were homogeneously dispersed on the surface of γ- Fe 2 O 3 (average diameter : 26 nm) without aggregation. Au nanoparticles are known to selectively adsorb the molecules having sulfur. Aiming at the uses for magnetic carriers of specific biomolecules, we employed prepared composite nanoparticles for selective separation of biomolecules and estimated their adsorption properties. The composite nanoparticles exhibited a high affinity with glutathione, a tripeptide with mercapto group, so that separation and manipulation of glutathione in aqueous solutions could be performed by applying an external magnetic field. Magnetic separations of amino acids were also investigated. Composite nanoparticles were mixed with amino acid standard solution containing 17 kinds of amino acids and their magnetic separations were carried out by applying an external magnetic field. It was found that adsorption amounts of methionine and cystine, containing internal sulfur were larger than other amino acids. The adsorbed amounts of sulfur containing amino acids increased with relative amount of Au in the composite nanoparticles.


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.


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