Isolation, purification, and characterization of a new enzyme from Pseudomonas sp. M-27, carboxypeptidase G3.

@article{Yasuda1992IsolationPA,
  title={Isolation, purification, and characterization of a new enzyme from Pseudomonas sp. M-27, carboxypeptidase G3.},
  author={Noriko Yasuda and Mikio Kaneko and Yoshinobu Kimura},
  journal={Bioscience, biotechnology, and biochemistry},
  year={1992},
  volume={56 10},
  pages={1536-40}
}
A new type of carboxypeptidase was found in a strain of Pseudomonas sp. M-27 isolated from soil. The cell-free extract, solubilized by colistin sulfate, was purified to homogeneity. This enzyme had a single peak with a molecular weight of 60,000 on a calibrated Superdex column and consisted of four subunits of identical molecular weights (M(r): 15,000). The enzyme hydrolyzed predominantly acidic peptides and N-acyl amino acids with Glu or Asp in the C-termini. This enzyme was not strongly… CONTINUE READING