Dipeptidyl Peptidase IV 来源于猪肾脏

The enzyme from sigma has been used in the determination of DPP-IV inhibitory activity of peptides in porcine skin gelatin hydrolysates.

Dipeptidyl peptidase IV from porcine kidney has been used in a study to investigate engraftment of donor cells following hepatocyte transplantation. Dipeptidyl peptidase IV from porcine kidney has also been used in a study to investigate the metabolism of glucagon-like peptide-2.

The pH optimum for the protease is 7.8-8.0. Dipeptidyl peptidase does not require activators. It is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, and diethyl p-nitrophenyl phosphate.

DPPIV has a post-proline dipeptidyl aminopeptidase activity that hydrolyzes N-terminal dipeptides from the unsubstituted N-terminus of peptides with the sequence of X-Pro-Z and X-Ala-Z. Where X is a nonspecific residue at the N terminus and Z cannot be proline or hydroxyproline.

Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N- and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18.3% carbohydrates, which the glycan composition is 0.9% fucose, 3.4% mannose, 5.1% galactose, 8.2% glucosamine, and 0.7% sialic acid. DPPIV is highly expressed on endothelial cells, epithelial cells, and lymphocytes. It is also present in plasma in its soluble form.

Lyophilized powder containing Tris buffer salts

One unit will produce 1.0 μmole of p-nitroaniline from Gly-L-Pro p-nitroanilide per min in 100 mM Tris-HCl at pH 8.0 at 37 °C.