Human serum dipeptidyl peptidase IV (DPPIV) and its unique properties

✍ Scribed by Hiroko Shibuya-Saruta; Yasushi Kasahara; Yohichi Hashimoto

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 671 KB
• Volume: 10
• Category: Article
• ISSN: 0887-8013
• DOI: 10.1002/(sici)1098-2825(1996)10:6<435::aid-jcla21>3.0.co;2-x

✦ Synopsis

Dipeptidyl peptidase IV (DPPIV, EC 3.4.1 4.5) has been purified 18,000-fold in a yield of 2.2% from human serum. Serum DPPIV, a serine enzyme with an apparent mass of 250 kDa, consists of two identical subunits with an apparent mass of 100 kDa and is inhibited by DPPIV-specific inhibitor Diprotin A and also by p-chloromercuribenzoate (p-CMB), 2-mercaptoethanol, HgCI2, CdC12, SrC12, and ZnCI2. One of the remarkable properties of DPPIV is that its activity is greatly enhanced by Gly-X (X: especially, Gly, Gln, Glu and Ser) dipeptides. Gly-X dipeptides increase not only an apparent Km