TY - JOUR T1 - pH Induced structural alterations in an aspartic protease from Vigna radiata indicating an alkali induced molten globule state JF - International Journal of Biological Macromolecules Y1 - 2008 A1 - Kulkarni, Aarohi A1 - Gaikwad, Sushama M. A1 - Rao, Mala KW - Alkali induced molten globule KW - Plant aspartic protease KW - Structural transitions AB -

pH-dependent transitions in secondary and tertiary structure are described for a plant aspartic protease from Vigna radiata. The enzyme was pH stable with pH optima of 3.0. The Lineweaver Burk analysis at various pH yielded pK(a) values of 3.3 and 4.29 indicating acidic amino acids at the active site of the enzyme. The structural changes exemplified compact secondary structure collapsed tertiary structure and exposure of hydrophobic patches at pH 10. The changes at pH 10 are typical of a molten globule state. This alkali induced molten globule is novel since acid induced molten globule state is more reported. (C) 2008 Elsevier B.V. All rights reserved.

PB - ELSEVIER SCIENCE BV CY - PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS VL - 43 IS - 4 U3 - Foreign U4 - 2.502 ER -