High impact information on NSC11772

• Along this line, a set of 58 imidazolidine-2,4-dione and 2-thioxoimidazolidin-4-one derivatives was evaluated as FAAH inhibitors [1].
• Hydrolysis with acetohydroxamate as reported originally by Stark [(1968) Biochemistry 7, 1796] was found to give excellent cleavage of the terminal thiohydantoin amino acid, but also led to the formation of stable hydroxamate esters of the shortened peptide which are poorly suited for subsequent rounds of degradation [2].
• Acid hydrolysis, using 6 N HCl, of globin from control and exposed rats caused cyclization of the valine-lysine thiourea cross-link in treated rats to isopropyl norleucyl thiohydantoin [3].
• Derivatized isopropyl norleucyl thiohydantoin obtained from CS2-treated rats displayed a cumulative dose response and was detectable at the lowest exposure (50 ppm, 2 weeks) at levels of approximately 50 pmol/g of globin [3].
• The thiohydantoin amino acid is identified by on-line high performance liquid chromatography using a Phenomenex Ultracarb 5 ODS(30) column and a triethylamine/phosphoric acid buffer system containing pentanesulfonic acid [4].

Biological context of NSC11772

• The sequencing procedure consists of converting the C-terminal amino acid into a thiohydantoin (TH) derivative, followed by transformation of the TH into a good leaving group by alkylation [5].
• Glycosylation of 2-thiohydantoin derivatives. Synthesis of some novel S-alkylated and S-glucosylated hydantoins [6].

Anatomical context of NSC11772

• The cytotoxicity of the 2-thiohydantoin derivatives to rat embryo fibroblasts (F2408) in vitro was determined, and the effects of these compounds on intracellular free Ca2+, [Ca2+]i, were measured by spectrofluorophotometry [7].

Associations of NSC11772 with other chemical compounds

• Based on the results of the study, combination of response surface mapping with Derringer's desirability function allows to predict the best operating condition in micellar liquid chromatography of phenyl thiohydantoin amino acids with respect to resolution and analysis time [8].
• Unlike formation of peptidylthiohydantoins with the other 19 commonly occurring amino acids in which cyclization to a thiohydantoin is concomitant with loss of a proton from the amide nitrogen, proline has no amide proton and as a result the newly formed proline thiohydantoin contains an unprotonated ring nitrogen [9].
• The reaction of DPP-ITC/pyridine with C-terminal proline rapidly forms an acyl isothiocyanate which is capable of forming a quaternary amine containing thiohydantoin [9].
• Glycine at the carboxy-terminus was derivatized to form 2-thiohydantoin, which was then separated and quantified by reverse phase HPLC [10].
• Proton magnetic resonance spectra of methylthiohydantoin (3-methyl-2-thiohydantoin), thiohydantoin (2-thiohydantoin), and hydantoin derivatives of amino acids were studied in dimethyl sulfoxide-d6 [11].

Gene context of NSC11772

• Employing sensitive high-performance liquid chromatography for the identification of amino acid thiohydantoin derivatives (PTH and DABTH), both methods were capable of sequencing immobilized peptides or proteins at the subnanomole levels [12].

Analytical, diagnostic and therapeutic context of NSC11772

• Improved initial yields in C-terminal sequence analysis by thiohydantoin chemistry using purified diphenylphosphoryl isothiocyanate: NMR evidence for a reaction intermediate in the coupling reaction [13].
• In order to apply this methodology to the analysis of proteins, the thiohydantoin derivatives of amino acids were synthesized and separated by reverse-phase HPLC [14].
• Thin-layer chromatography of phenyl thiohydantoin derivatives of amino acids on silica gel thin layers impregnated with zinc salts and some metal sulphates [15].

References