The purification and characterization of a Bacillus stearothermophilus methionine aminopeptidase (MetAP).

@article{Chung2002ThePA,
  title={The purification and characterization of a Bacillus stearothermophilus methionine aminopeptidase (MetAP).},
  author={Jae Min Chung and Il Yup Chung and Young Seek Lee},
  journal={Journal of biochemistry and molecular biology},
  year={2002},
  volume={35 2},
  pages={
          228-35
        }
}
Methionine aminopeptidase (MetAP) catalyzes the removal of an amino-terminal methionine from a newly synthesized polypeptide. The enzyme was purified to homogeneity from Bacillus stearothermophilus (KCTC 1752) by a procedure that involves heat precipitation and four sequential chromatographs (including DEAESepharose ion exchange, hydroxylapatite, Ultrogel AcA 54 gel filtration, and Reactive red 120 dye affinity chromatography). The apparent molecular masses of the enzyme were 81,300 Da and 41… 

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