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Purification and Characterization of a Hygromycin B Phosphotransferase From Streptomyces Hygroscopicus

Purification and Characterization of a Hygromycin B Phosphotransferase From Streptomyces Hygroscopicus

M Zalacain, J M Pardo, A Jiménez

Eur J Biochem. 1987 Jan 15;162(2):419-22.

PMID: 3026811

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 single protein band (41 kDa) when subjected to polyacrylamide 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 microM for hygromycin B and ATP, respectively, were deduced.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP31282049	Hygromycin B from Streptomyces hygroscopicus		31282-04-9	Price

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