Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: Nucleotide specificity, pH optimum, and the separation of two electrophoretic variants-Reference-Cited by-同舟云学术

Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: Nucleotide specificity, pH optimum, and the separation of two electrophoretic variants

Published:1984-04 Issue:1 Volume:230 Page:250-263
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

van Pelt Jean E.,Northrop Dexter B.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference26 articles.

1. Control of complex metal ion equilibria in biochemical reaction systems. Intrinsic and apparent stability constants of metal-adenine nucleotide complexes.

2. Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa.

3. R-factor mediated gentamicin resistance: A new enzyme which modifies aminoglycoside antibiotics

4. Multiple antibiotic resistance and capsular types of gentamicin-resistant Kiebsiella aerogenes

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