High impact information on NSC 49244

• Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletal muscle phosphorylase kinase: localization by conversion to S-ethylcysteine and by tandem mass spectrometry [1].
• To discern between these possibilities and to identify the phosphorylation sites, the protein was purified from serum-stimulated cells and cleaved with endo Lys-C, and the single endo Lys-C phosphorylated peptide was isolated and sequenced following conversion of all the phosphorylated serines to S-ethylcysteine [2].
• The stoichiometry of phosphate in phosphorylated prolactin was 1.4:1 when determined by amino acid analysis after preparation of the S-ethylcysteine derivative [3].
• Among water-soluble compounds, SAC, S-ethylcysteine (SEC), and S-propylcysteine (SPC) inhibited cholesterol synthesis by 40--60% compared with 20--35% by gamma-glutamyl-S-allylcysteine (GSAC), gamma-glutamyl-S-methylcysteine (GSMC) and gamma-glutamyl-S-propylcysteine (GSPC) [4].
• The number of S-ethylcysteine residues in a peptide can be quantified at the picomolar level, following acid hydrolysis and conversion to the phenylthiocarbamyl derivative [5].

Biological context of NSC 49244

• A trend was observed which implies that for CI2 the original methionine residue or its isostere S-ethylcysteine are most effective residues at this position and not alanine as might have been expected from the substrate specificity [6].

Associations of NSC 49244 with other chemical compounds

• A novel S-alkylcysteine derivative, S-ethylcysteine sulfoxide (ethiin), not previously reported to occur in Allium species, was found in some of the samples examined [7].
• The protective effects of six organosulfur compounds (DAS, diallyl sulfide; DADS, diallyl disulfide; SAC, S-allylcysteine; SEC, S-ethylcysteine; SMC, S-methylcysteine; SPC, S-propylcysteine) against further oxidation and glycation in these already partially oxidized and glycated samples were studied [8].
• Using a combination of S-ethylcysteine derivatization, sequence analysis, and mass spectrometric analysis, the phosphorylation sites of ovine (SerP151 and SerP168), caprine (SerP151 and SerP168), and bovine (SerP149) caseinomacropeptides have been localized [9].
• Addition of 10(-2) M L-cysteine, L-cystine, or S-ethyl-L-cysteine to a synthetic medium containing xylose as the sole carbon source did not decrease ochratoxin production by Aspergillus ochraceus [10].
• In the column effluent S-ethyl-L-cysteine is derivatized by o-phthaldialdehyde and the reaction product is detected by fluorescence measurement [11].

References