Purification and biochemical characterization of a novel secretory dipeptidyl peptidase IV from porcine serum

Kumar, Divya and Hamse, Vivek K. and Neema, K. N. and Shubha, Priya Babu and Chetan, D. M. and Shivananju, Nanjunda Swamy (2020) Purification and biochemical characterization of a novel secretory dipeptidyl peptidase IV from porcine serum. Molecular and Cellular Biochemistry, 471 (1-2). pp. 71-80. ISSN 0300-8177

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Abstract

Purification of DPP-IV enzyme from porcine serum, is presented in this study for the first time. The high molecular weight DPP-IV from porcine serum was fractioned using Sephadex G-75 gel filtration followed by DEAE Sephadex anion exchange and Sephadex G-100 gel filtration chromatography columns with a final yield of 11.25%. The SDS-PAGE of the purified sample showed a single band of molecular mass nearing 160 kDa. Distinct single band was observed after PAS staining confirmed it to be a glycoprotein. The purified enzyme showed an optimum pH and temperature of 8 and 37 degrees C, respectively. The enzyme effectively cleaved fluorogenic substrate Gly-Pro-AMC with Km and Vmax of 4.578 mu M and 90.84 nmoles/min, respectively. Purified DPP-IV activity was inhibited by Diprotin A with an IC(50)value of 8.473 mu M. Among the three plant extracts used to study DPP-IV inhibition, the aqueous hot extract ofTerminalia chebulashowed the highest inhibition of 87.19%, followed by the aqueous cold extract ofMomordica carantia, ( 31.6%) andAzadirachta indica(34.16%) at the concentration of 25 mu g.

Item Type:	Article
Subjects:	C Chemical Science > Chemistry
Divisions:	Department of > Chemistry
Depositing User:	Mr Umendra uom
Date Deposited:	23 Feb 2021 06:25
Last Modified:	23 Feb 2021 06:25
URI:	http://eprints.uni-mysore.ac.in/id/eprint/15561

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