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Purification and biochemical characterization of a novel secretory dipeptidyl peptidase IV from porcine serum.
Kumar, Divya; Hamse, Vivek K; Neema, K N; Babu Shubha, Priya; Chetan, D M; Shivananju, Nanjunda Swamy.
Afiliação
  • Kumar D; Department of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS TI Campus, Mysuru, Karnataka, 570006, India.
  • Hamse VK; Faculty of Natural Sciences, Adichunchanagiri University, Bellur Cross, B.G. Nagara, Mandya, Karnataka, India.
  • Neema KN; Department of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS TI Campus, Mysuru, Karnataka, 570006, India.
  • Babu Shubha P; Department of Studies in Chemistry, University of Mysore, Manasagangothri, Mysuru, Karnataka, 570006, India.
  • Chetan DM; Department of Biotechnology, NMAM Institute of Technology, Nitte, Karkala Taluk, Udupi, Karnataka, 574110, India.
  • Shivananju NS; Department of Biotechnology, Sri Jayachamarajendra College of Engineering, JSS Science and Technology University, JSS TI Campus, Mysuru, Karnataka, 570006, India. nanjundaswamy@sjce.ac.in.
Mol Cell Biochem ; 471(1-2): 71-80, 2020 Aug.
Article em En | MEDLINE | ID: mdl-32577945
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 °C, respectively. The enzyme effectively cleaved fluorogenic substrate Gly-Pro-AMC with Km and Vmax of 4.578 µM and 90.84 nmoles/min, respectively. Purified DPP-IV activity was inhibited by Diprotin A with an IC50 value of 8.473 µM. Among the three plant extracts used to study DPP-IV inhibition, the aqueous hot extract of Terminalia chebula showed the highest inhibition of 87.19%, followed by the aqueous cold extract of Momordica carantia, ( 31.6%) and Azadirachta indica (34.16%) at the concentration of 25 µg.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Dipeptidil Peptidase 4 / Dipeptídeos / Ensaios Enzimáticos Idioma: En Revista: Mol Cell Biochem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Dipeptidil Peptidase 4 / Dipeptídeos / Ensaios Enzimáticos Idioma: En Revista: Mol Cell Biochem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Índia