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Título : Purification and characterization of a hygromycin B phosphotransferase from Streptomyces hygroscopicus
Autor : Zalacaín, Magdalena, Pardo, José M., Jiménez Díaz, Antonio
Fecha de publicación : 1987
Editor: Wiley-Blackwell
Citación : European Journal of Biochemistry 162(2): 419-422 (1987)
Resumen: A hygromycin B phosphotransferase activity from Streptomyces hygroscopicus has been highly purified by ammonium sulphate fractionation followed by affinity column chromatography through Sepharose-6B- hygromycin-B.The combined active fractions showed a singleprotein band (41 kDa) when subjected to polyacryl- amide gel electrophoresis in the presence of sodium dodecyl sulphate. When gel electrophoresis was performed under non-denaturing conditions, the single protein band promoted in situ phosphorylation of hygromycin B, indicating that this protein corresponded to the purified hygromycin B phosphotransferase. The enzyme has been purified 236-fold and approximate Km values of 0.56 pM and 36.4 pM for hygromycin B and ATP, respectively, were deduced.
Descripción : 4 pages, 4 figures, 1 table, 20 references.
Versión del editor: http://dx.doi.org/10.1111/j.1432-1033.1987.tb10618.x
URI : http://hdl.handle.net/10261/57133
ISSN: 0014-2956
DOI: 10.1111/j.1432-1033.1987.tb10618.x
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