Reversibility in protein folding: effect of β-cyclodextrin on bovine serum albumin unfolded by sodium dodecyl sulphate

2013 ◽  
Vol 15 (23) ◽  
pp. 9375 ◽  
Author(s):  
Uttam Anand ◽  
Saptarshi Mukherjee
Keyword(s):  
Protein Folding ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Sodium Dodecyl

scholarly journals The binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios

1974 ◽  
Vol 137 (3) ◽  
pp. 575-578 ◽  
Author(s):  
Geoffrey Allen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Weight Ratio ◽  
Binding Ratio ◽  
High Binding

The extent of binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios was investigated by gel filtration. The weight ratio of bound sodium dodecyl sulphate to bovine serum albumin increases with the NaCl concentration, and, except at low salt concentrations, with the concentration of sodium dodecyl sulphate. In the presence of 1.0g of sodium dodecyl sulphate/l, the binding ratio varied from 1.0 (at 0.04m-Na+) to 2.2 (at 0.44m-Na+). In the presence of 0.24m-Na+, the binding ratio increased with sodium dodecyl sulphate concentration, from 0.9 (0.2g of sodium dodecyl sulphate/l) to 2.0 (5g of sodium dodecyl sulphate/l), at 26°C, in a dilute sodium phosphate buffer. No significant dependence of the binding ratio upon temperature in the range 26–45°C was observed. These results differ from those of Reynolds & Tanford (1970a) obtained by equilibrium dialysis.

scholarly journals Characterization of Choreospondias axillaris (Lapsi) fruit protease

2009 ◽  
Vol 3 ◽  
Author(s):  
Sabin Prajapati ◽  
Samanta Sharma ◽  
Vishwanath P Agrawal
Keyword(s):  
Acetic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Protein Concentration ◽  
Sodium Dodecyl ◽  
Km Value ◽  
Deciduous Fruit

A catalytically powerful protease from Choreospondias axillaris (Lapsi) fruit has been reported. C. axillaris (Lapsi) is dioecious, deciduous fruit bearing tree. The protease extracted from the pulp of the fruit is highly thermo stable, autoclavable and extreme acidic and basic pH resistant. Its activity was retained even after multiple trichloro acetic acid (TCA) precipitation. The proteolytic activity of the protease increased linearly up to protein concentration of 62.28μg. It possesses a Km value of 13.09 μM and Vmax 15.87 pmoles/min for bovine serum albumin (BSA) as a substrate. Sodium Dodecyl Sulphate (SDS) activated the proteolytic activity.DOI: 10.3126/ijls.v3i0.2386Int J Life Sci Vol.3 2009 p.19-26

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