Journal of Chromatography & Separation Techniques
Open Access

Bilqees B

Publications

• Research Article
  Purification and Biochemical Characterization of a Cystatin-Like Thiol Proteinase Inhibitor from Cicer arietinum (Chickpea)
  Author(s): Sheraz AB, Waseem FB, Aaliya S, Shahnawaz KM, Rizwan HK and Bilqees B* Sheraz AB, Waseem FB, Aaliya S, Shahnawaz KM, Rizwan HK and Bilqees B*
  
  Cystatins are thiol proteinase inhibitors ubiquitously present in many plants as well as animal tissues. In the present study, a cystatin like a thiol proteinase inhibitor was isolated from chickpea using ammonium sulfate fractionation (40-60%) and gel filtration chromatography on a Sephacryl S-100 HR column with 21.09% yield and fold purification of 78.89. It gave a molecular mass of about 25.3 kDa as determined by SDS-PAGE, Dynamic Light Scattering (DLS), and from its gel filtration behavior. The inhibitor was found to have very low carbohydrate content (0.34%) and meager amount (1.45%) of sulfhydryl content. The Stokes radius, frictional, diffusion and sedimentation coefficients of CPC were 4.299 × 10-8 g/s, 22.82 Å, 12.68 × 10-7 cm2 s-1 and 2.64 S, respectively. Kinetic analysis of CPC with thiol proteinases (papain, fi.. View More»
  DOI: 10.4172/2157-7064.1000387

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