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Open Access item 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
ISSN:0014-2956
E-ISSNmetadata.dc.identifier.doi = DOI:1432-1033
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Appears in Collections:(IRNAS) Artículos

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