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Amino pterin

Successful fusion (2) is a rare event, but the frequency can be improved by adding polyethylene glycol (PEG). To obtain only successfully fused cells, incubation is required for an extended period in a primary culture with HAT medium (3), which contains hypoxan-thine, aminopterin, and thymidine. Amino-pterin, an analogue of dihydrofolic acid, competitively inhibits dihydrofolate reductase and thus inhibits the synthesis of dTMP (see p. 402). As dTMP is essential for DNA synthesis, myeloma cells cannot survive in the presence of aminopterin. Although spleen cells are able to circumvent the inhibitory effect of aminopterin by using hypoxanthine and thymidine, they have a limited lifespan and die. Only hybridomas survive culture in HAT medium, because they possess both the immortality of the myeloma cells and the spleen cells metabolic side pathway. [Pg.304]

FOLIC ACID, AMINO PTERIN AND METHOTREXATE ANALOGUES... [Pg.100]

Die beim Aufarbeiten axis Organismenextrakten isolierten 6-Amino-pterin (XXII) und Pterin-6-sulfonsaure (XXIV) konnen dementspre-chend Artefakte sein, die vielleicht in Gegenwart von Ammoniak bzw. Sulfitsalzen aus natiirlichen hydrierten Derivaten entstanden sind (18,59). [Pg.134]

Aminopteridine is the most sensitive to acid hydrolysis, and 6-amino- and 6-dimethyl-amino-pteridine are also hydrolyzed, even by cold 0.0IN hydrochloric acid, too rapidly for accurate determination of the cation form (52JCS1620). 2-Amino- and 4-amino-pteridine are not readily attacked by IN HCl at 20 °C but at 100 °C the former compound is destroyed and the latter converted into pteridin-4-one (5UCS474). 2,4-Diaminopteridine can be hydrolyzed by refluxing in 6N HCl for 30 minutes to 2-aminopteridin-4-one (pterin 2) and after... [Pg.293]

Various 6- and 7-methyl- and 6,7-dimethyl-pteridines bearing either oxo or amino groups in the 2- and 4-positions can be oxidized to the corresponding carboxylic acids by alkaline potassium permanganate on heating. Various lumazine and pterin mono- and di-carboxylic acids have been prepared in this way (48JA3026, 78CB3790). [Pg.302]

Pterin, 4-amino — see Folic acid, 4-amino-4-deoxy-Pterin, 6-amino-structure, 3, 276 Pterin, 7-amino-structure, 3, 276 Pterin, 6-arylthio-reactivity, 3, 299 Pterin, 6-(l-carboxyethoxy)-synthesis, 3, 309 Pterin, 6-carboxy-7-hydroxy-properties, 3, 277 Pterin, 7-carboxy-6-hydroxy-properties, 3, 277 Pterin, 6-chloro-nucleophilic substitution, 3, 292 synthesis, 3, 290... [Pg.755]

Pterin-4-one, 2-amino-stnicture, 3, 273 Pterin-7-one, 2,4-dimethoxy-hydrolysis, 3, 299 Pterin-6-ones reactions... [Pg.757]

Pterin-dependent amino acid hydroxylases 96CRV2659. [Pg.238]

The aldehyde oxidoreductase from Desulfovibrio gigas shows 52% sequence identity with xanthine oxidase (199, 212) and is, so far, the single representative of the xanthine oxidase family. The 3D structure of MOP was analyzed at 1.8 A resolution in several states oxidized, reduced, desulfo and sulfo forms, and alcohol-bound (200), which has allowed more precise definition of the metal coordination site and contributed to the understanding of its role in catalysis. The overall structure, composed of a single polypeptide of 907 amino acid residues, is organized into four domains two N-terminus smaller domains, which bind the two types of [2Fe-2S] centers and two much larger domains, which harbor the molybdopterin cofactor, deeply buried in the molecule (Fig. 10). The pterin cofactor is present as a cytosine dinucleotide (MCD) and is 15 A away from the molecular surface,... [Pg.398]

D. desulfuricans is able to grow on nitrate, inducing two enzymes that responsible for the steps of conversion of nitrate to nitrite (nitrate reductase-NAP), which is an iron-sulfur Mo-containing enzyme, and that for conversion of nitrite to ammonia (nitrite reduc-tase-NIR), which is a heme-containing enzyme. Nitrate reductase from D. desulfuricans is the only characterized enzyme isolated from a sulfate reducer that has this function. The enzyme is a monomer of 74 kDa and contains two MGD bound to a molybdenum and one [4Fe-4S] center (228, 229) in a single polypeptide chain of 753 amino acids. FXAFS data on the native nitrate reductase show that besides the two pterins coordinated to the molybdenum, there is a cysteine and a nonsulfur ligand, probably a Mo-OH (G. N. George, personal communication). [Pg.404]

Pterins — These are pigments derived from pteridine skeletons. All natural pterins are 2-amino-4-hydroxypteridines bearing various substituents at Cg and C7 and having different oxidation states of N5 and Ng. [Pg.107]


See other pages where Amino pterin is mentioned: [Pg.309]    [Pg.198]    [Pg.918]    [Pg.309]    [Pg.309]    [Pg.2415]    [Pg.99]    [Pg.198]    [Pg.27]    [Pg.309]    [Pg.198]    [Pg.918]    [Pg.309]    [Pg.309]    [Pg.2415]    [Pg.99]    [Pg.198]    [Pg.27]    [Pg.43]    [Pg.264]    [Pg.273]    [Pg.277]    [Pg.277]    [Pg.277]    [Pg.279]    [Pg.281]    [Pg.293]    [Pg.294]    [Pg.294]    [Pg.295]    [Pg.297]    [Pg.301]    [Pg.305]    [Pg.305]    [Pg.308]    [Pg.312]    [Pg.318]    [Pg.318]    [Pg.320]    [Pg.323]    [Pg.755]    [Pg.756]    [Pg.563]    [Pg.602]    [Pg.60]    [Pg.93]    [Pg.93]   
See also in sourсe #XX -- [ Pg.40 ]




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