Purification and properties of ampicillin acylase from Pseudomonas melanogenum.

@article{Kim1990PurificationAP,
  title={Purification and properties of ampicillin acylase from Pseudomonas melanogenum.},
  author={Dae Jung Kim and Si Myung Byun},
  journal={Biochimica et biophysica acta},
  year={1990},
  volume={1040 1},
  pages={
          12-8
        }
}
Ampicillin acylase, which is known to have a novel substrate spectrum, was purified to homogeneity from Pseudomonas melanogenum by the crude extract preparation and chromatography with S-Sepharose, hydroxyapatite, CM-cellulose C-52, and CM-Sepharose. The molecular weight of the native enzyme was calculated to be 146,000 by Protein PAK-300 sw HPLC chromatography. SDS-polyacrylamide gel electrophoresis revealed that the enzyme consisted of two identical subunits with a molecular weight of 72,000… CONTINUE READING
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