Purification of Thymidylate Synthetase from Ehrlich Ascites Carcinoma Cells
نویسندگان
چکیده
منابع مشابه
Studies with GMP synthetase from Ehrlich ascites cells. Purification, properties, and interactions with nucleotide analogs.
GMP synthetase has been purified 57-fold from Ehrlich ascites cells. The enzyme was found to be stable and to have an approximate molecular weight of 85,000 (determined by gel filtration). Its activity was stimulated by dithiothreitol and inhibited by 2-mercaptoethanol, p-chloromercuribenzoate, and hydroxylamine. Both ammonia and glutamine could serve as amino group donors. While none of the 10...
متن کاملStudies with GMP Synthetase from Ehrlich Ascites Cells
GMP synthetase has been purified 57-fold from Ehrlich ascites cells. The enzyme was found to be stable and to have an approximate molecular weight of 85,000 (determined by gel filtration). Its activity was stimulated by dithiothreitol and inhibited by 2-mercaptoethanol, p-chloromercuribenzoate, and hydroxylamine. Both ammonia and glutamine could serve as amino group donors. While none of the 10...
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Interferon production was induced in mouse Ehrlich ascites tumor cells by infection with Newcastle disease virus. The interferon produced was purified by precipitation with ammonium sulfate, chromatography on carboxymethyl-Sephadex, treatment with blue dextran and polyethylene glycol, gel filtration on Bio-Gel P-60 and Bio-Gel P-200, chromatography on phosphocellulose, isoelectric focusing, and...
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Anl i-tumor sera are now being extensively used in investigations of the activities of neoplasms (e.g. 4-7, 9-13, 15). I t is already known (7), concerning their effects on the biochemical activities of tumors, that Ehrlich ascites carcinoma cells, treated with their antisera in the presence of comp]ement, lose their capacity to respire in the presence of glucose but not in the presence of succ...
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The enzyme, thymidylate synthetase, catalyzes the methylation of deosyuridylate to thymidylate, with formaldehyde as the source of the methyl group, in the presence of tetrahydrofolate. Some of the properties of this enzyme system in crude soluble protein extracts of rat thymus have previously been reported (1). Reports have also appeared of this enzyme reaction in Escherichia cozi (2, 3). The ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45860-2