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- Title
Cystatin like thiol proteinase inhibitor from pancreas of Capra hircus: purification and detailed biochemical characterization.
- Authors
Priyadarshini, Medha; Bano, Bilqees
- Abstract
A thiol proteinase inhibitor from Capra hircus (goat) pancreas (PTPI) isolated by ammonium sulphate precipitation (20–80%) and gel filtration chromatography on Sephacryl S-100HR, with 20.4% yield and 500-fold purification, gave molecular mass of 44 kDa determined by its electrophoretic and gel filtration behavior, respectively. The stokes radius, diffusion and sedimentation coefficients of PTPI were 27.3 Ǻ, 7.87 × 10−7 cm2 s−1 and 3.83 s, respectively. It was stable in pH range 3–10 and up to 70°C (critical temperature, Ea = 21 kJ mol−1). Kinetic analysis revealed reversible and competitive mode of inhibition with PTPI showing the highest inhibitory efficiency against papain ( K i = 5.88 nM). The partial amino acid sequence analysis showed that it shared good homology with bovine parotid and skin cystatin C. PTPI possessed 17.18% α helical content assessed by CD spectroscopy. The hydropathy plot of first 24 residues suggested that most amino acids of this stretch might be in the hydrophobic core of the protein.
- Subjects
THIOLS; CYSTATINS; PROTEINASES; GOATS; PANCREAS
- Publication
Amino Acids, 2010, Vol 38, Issue 4, p1001
- ISSN
0939-4451
- Publication type
Article
- DOI
10.1007/s00726-009-0308-x