Progressive Agriculture
  • Year: 2006
  • Volume: 6
  • Issue: 2

Isozyme profile and kinetic properties of partially purified superoxide dismutase from tomato fruit

  • Author:
  • Sunil Kumar, Santosh Dhillon, Dharam Singh, Randhir Singh, Mukesh Kumar
  • Total Page Count: 5
  • Page Number: 130 to 134

* Department of Molecular Biology & Biotechnology, Maharana Pratap University of Agriculture & Technology, Udaipur

** Department of Biotechnology and Molecular Biology, College of Basic Sciences and Humanities CCS Haryana Agricultural University, Hisar-125004

Plant Biochemistry and Molecular Biology Laboratory. Department of Biochemistry, College of Basic Sciences and Humanities

Online published on 6 September, 2012.

Abstract

Superoxide dismutase (SOD) from tomato (Lycopersicon esculentum Millo) fruit was partially purified and isozyme profile determined on PAGE using enzyme specific staining. Ammonium sulphate fraction (35–75%) showed four isozymes, molecular weights 66.0, 47.9, 37.1 and 35.5 Kda, respectively, of which 37.1 Kda isozyme appeared as major band. The major isozyme was further purified and characterized for kinetic parameters which showed maximum activity at 60 μM and 3.0 μM of NBT and riboflavin, respectively. The per cent inhibition of NBT photo reduction was linear upto 68% with increasing enzyme concentration. The enzyme had pH and temperature optima of 7.8 and 50°C, respectively, and an incubation time of 45 min on light exposure.

Keywords

Incubation time, izozyme profile, percent inhibition, superoxide dismutase, tomato fruit