scholarly journals Metabolism of Sulfur-containing Amino Acids by Pregnant Merino Ewes

1988 ◽  
Vol 41 (2) ◽  
pp. 247 ◽  
Author(s):  
AJ Williams ◽  
R Murison ◽  
J Padgett

The availability and utilization of cystine and methionine were measured in single-bearing Merino ewes on three occasions, approximately 90, 110 and 130 days after mating, and the effects on these traits of sulfur amino acids (SAA) infused into the abomasum were also measured. Two levels of SAA were infused containing 0�5 or 1�0 g day-i organic sulfur with DL-methionine contributing two-thirds and L-cystine onethird of the supplementary sulfur. The quantity of the diet offered was increased at each occasion so as to maintain maternal liveweight.

Author(s):  
Nikola Sobot ◽  
Tanja Sobot ◽  
Katarina Radonjic ◽  
Tamara Nikolic Turnic ◽  
Anica Petkovic ◽  
...  

AbstractSulfur-containing amino acids are integral part of molecular mechanisms which underlie many aspects of cellular function and homeostasis, facilitated by reversible changes in oxidation states of sulfur atoms. Dysregulation of these pathways is associated with diverse pathologies, notably of the cardiovascular system, which are typically characterized by inappropriate plasma levels of sulfur-containing amino acids. The aim of this study was to assess the acute, direct effects of sulfur-containing amino acids and inorganic NaHS, as H2S donor, on cardiodynamic parameters in homocysteine treated rats. Moderate hyperhomocysteinemia did not cause significant decrease in myocardial contractility, but our findings suggest that NaHS and L-methionine cause negative effects on cardiac function in hearts of the rats treated with homo-cysteine, even in a single administration. Further investigations need to be carried out with purpose of better understanding and highlightening the impact of Hcy and sulphur amino acids on cardiac function.


Molbank ◽  
10.3390/m1147 ◽  
2020 ◽  
Vol 2020 (3) ◽  
pp. M1147
Author(s):  
Giovanna Speranza ◽  
Marco Rabuffetti ◽  
Nikolina Vidović ◽  
Carlo F. Morelli

γ-Glutamyl derivatives of sulfur amino acids have been prepared in multigram scale starting from readily available starting materials. The synthesis comprises two one-pot operations, both consisting of two reactions. In the first operation, N-phtaloyl-l-glutamic acid anhydride is obtained from l-glutamic acid and phtalic anhydride. In the second one, N-phtaloyl-l-glutamic acid anhydride is used to acylate amino acids and the N-phtaloyl protecting group is removed. The described approach offers a viable entry to γ-glutamyl derivatives of sulfur-containing amino acids with flavor-enhancer and nutraceutical properties.


Synthesis ◽  
2021 ◽  
Author(s):  
Sparta Youssef-Saliba ◽  
Yannick Vallée

Two sulfur containing amino acids are included in the list of the 20 classical protein amino acids. A methionine residue is introduced at the start of the synthesis of all current proteins. Cysteine, thanks to its thiol function, plays an essential role in a very large number of catalytic sites. Here we present what is known about the prebiotic synthesis of these two amino acids and homocysteine, and we discuss their introduction into primitive peptides and more elaborate proteins.


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).


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