Escherichia coli Murein Transglycosylase
- 1 January 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 103 (2), 277-281
- https://doi.org/10.1111/j.1432-1033.1980.tb04312.x
Abstract
E. coli murein transglycosylase, a potential autolysin which splits the sugar chains of the murein sacculus, was rapidly purified from a crude cell extract by sequential chromatography on columns of blue Sepharose and poly(U)-Sepharose. In accordance with the binding to blue Sepharose and poly(U)-Sepharose, the transglycosylase is inhibited by Cibacron blue F3G-A, the affinity ligand of blue Sepharose, and also by polynucleotides, the latter with varying efficiency. Among the polynucleotides tested, single-stranded DNA was one of the most potent inhibitors. When bound to a blue Sepharose column, transglycosylase could be displaced from the column with single-stranded DNA. Taken together, these results point to a polynucleotide binding area on the transglycosylase molecule. Some aspects of the blue Sepharose affinity chromatography and the possible biological significance of the transglycosylase are discussed.This publication has 22 references indexed in Scilit:
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