Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs.

@article{Hinke2000DipeptidylPI,
  title={Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs.},
  author={Simon A. Hinke and John Andrew Pospisilik and Hans Ulrich Demuth and S Mannhart and Kerstin K{\"u}hn-Wache and Torsten Andreas Hoffmann and Erica Nishimura and Raymond A. Pederson and Christopher H. S. McIntosh},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 6},
  pages={3827-34}
}
Over the past decade, numerous studies have been targeted at defining structure-activity relationships of glucagon. Recently, we have found that glucagon(1-29) is hydrolyzed by dipeptidyl peptidase IV (DPIV) to produce glucagon(3-29) and glucagon(5-29); in human serum, [pyroglutamyl (pGlu)(3)]glucagon(3-29) is formed from glucagon(3-29), and this prevents further hydrolysis of glucagon by DPIV (H.-U. Demuth, K. Glund, U. Heiser, J. Pospisilik, S. Hinke, T. Hoffmann, F. Rosche, D. Schlenzig, M… CONTINUE READING

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