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Título: | Expression of rat liver S-adenosylmethionine synthetase in Escherichia coli results in two active oligomeric forms |
Autor: | Álvarez, Luis; Mingorance, Jesús CSIC ORCID; Pajares, María A. CSIC ORCID ; Mato, José M. | Fecha de publicación: | 15-jul-1994 | Editor: | Portland Press Biochemical Society |
Citación: | Biochemical Journal 301(2): 557-561 (1994) | Resumen: | A cDNA containing the complete coding sequence for rat liver S-adenosylmethionine synthetase was cloned into the prokaryotic expression vector pT7-7 and expressed in Escherichia coli BL21(DE3). A major additional band corresponding to a protein of 48 kDa was detected on SDS/PAGE after induction with isopropyl beta-D-thiogalactopyranoside. This protein was distributed in both the soluble and insoluble fractions and accounted for approx. 30% of the total bacterial protein. The soluble enzyme was fully active, as revealed by assays in vitro of S-adenosylmethionine synthetase activity. In addition, transformed bacteria exhibited highly increased levels of intracellular S-adenosylmethionine. Two active forms of the recombinant enzyme, with apparent molecular masses of 210 kDa and 110 kDa, were detected when cytosolic extracts of the transformed cells were fractionated by gel-filtration chromatography. It is concluded that the expressed S-adenosylmethionine synthetase polypeptide assemble as tetramers and dimers. | Descripción: | 5 pages, 3 figures. | URI: | http://hdl.handle.net/10261/23949 | ISSN: | 0264-6021 |
Aparece en las colecciones: | (IIBM) Artículos |
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