The isolation and some properties of dipeptidyl peptidases II and III from porcine spleen.

@article{Lynn1991TheIA,
  title={The isolation and some properties of dipeptidyl peptidases II and III from porcine spleen.},
  author={K R Lynn},
  journal={The International journal of biochemistry},
  year={1991},
  volume={23 1},
  pages={47-50}
}
  • K R Lynn
  • Published 1991 in The International journal of biochemistry
1. Dipeptidyl peptidases (DPP) II and III from porcine spleen have been purified to homogeneity as assessed by disc gel electrophoresis, HPLC and chromatofocusing. 2. The enzyme are both inhibited by diisopropylfluorophosphate suggesting that the active site contains an essential serine residue, but they are also inhibited by a variety of other reagents. 3. The pI of DPP II is 4.8, that of DPP III, 4.0. 4. The former enzyme has a molecular weight of 97,000, the latter 66,000 and both are… CONTINUE READING