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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/57133
Title: Purification and characterization of a hygromycin B phosphotransferase from Streptomyces hygroscopicus
Authors: Zalacaín, Magdalena; Pardo, José M. ; Jiménez Díaz, Antonio
Issue Date: 1987
Publisher: Wiley-Blackwell
Citation: European Journal of Biochemistry 162(2): 419-422 (1987)
Abstract: 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.
Description: 4 pages, 4 figures, 1 table, 20 references.
Publisher version (URL): http://dx.doi.org/10.1111/j.1432-1033.1987.tb10618.x
URI: http://hdl.handle.net/10261/57133
DOI: 10.1111/j.1432-1033.1987.tb10618.x
ISSN: 0014-2956
E-ISSN: 1432-1033
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