The role of dipeptidyl peptidase IV in the cleavage of glucagon family peptides: in vivo metabolism of pituitary adenylate cyclase-activating polypeptide-(1–38)
L Zhu, C Tamvakopoulos, D Xie, J Dragovic… - Journal of Biological …, 2003 - ASBMB
Dipeptidyl peptidase IV (DP-IV) is a cell surface serine dipeptidase that is involved in the
regulation of the incretin hormones, glucagon-like peptide (GLP-1) and glucose-dependent
insulinotropic polypeptide (GIP). There is accumulating evidence that other members of the
glucagon family of peptides are also endogenous substrates for this enzyme. To identify
candidate substrates for DP-IV, a mass spectrometry-based protease assay was developed
that measures cleavage efficiencies (k cat/K m) of polypeptides in a mixture, using only a few …
regulation of the incretin hormones, glucagon-like peptide (GLP-1) and glucose-dependent
insulinotropic polypeptide (GIP). There is accumulating evidence that other members of the
glucagon family of peptides are also endogenous substrates for this enzyme. To identify
candidate substrates for DP-IV, a mass spectrometry-based protease assay was developed
that measures cleavage efficiencies (k cat/K m) of polypeptides in a mixture, using only a few …
