Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin.

@article{Lee1982DipeptidylaminopeptidaseIO,
  title={Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin.},
  author={Chung M. Lee and Solomon H Snyder},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 20},
  pages={12043-50}
}
The cytosolic dipeptidyl-aminopeptidase III (EC 3.4.14.4) from rat brain was partially purified using Arg-Arg-4-methoxy-beta-naphthylamide as a substrate. It was completely separated from aminopeptidase B on DEAE-Sephacel ion exchange chromatography. Similar to bovine pituitary dipeptidyl-aminopeptidase III, it has a pH optimum of 9, prefers Arg-Arg-4-methoxy-beta-naphthylamide as a substrate, and catalyzes the sequential release of dipeptides from the NH2 terminus of peptide substrates… CONTINUE READING

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