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Characterization of Acid-induced Unfolding Intermediates of Glucose/xylose Isomerase by S. A. Pawar; V. V. Deshpande is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Acid‐induced unfolding of the tetrameric glucose/xylose isomerase (GXI) from __Streptomyces__ sp. NCIM 2730 has been investigated using intrinsic fluorescence, fluorescence quenching, second derivative spectroscopy, hydrophobic dye (1‐anilino‐8‐naphthalene‐sulfonate) binding and CD techniques. The pH dependence of tryptophanyl fluorescence of GXI at different temperatures indicated the presence of two stable intermediates at pH 5.0 and pH 3.0. The pH 3.2 intermediate was a dimer and exhibited molten globule‐like characteristics, such as the presence of native‐like secondary structure, loss of tertiary structure, increased exposure of hydrophobic pockets, altered microenvironment of tyrosine residues and increased accessibility to quenching by acrylamide. Fluorescence and CD studies on GXI at pH 5.0 suggested the involvement of a partially folded intermediate state in the native to molten globule state transition. The partially folded intermediate state retained considerable secondary and tertiary structure compared to the molten globule state. This state was characterized by its hydrophobic dye binding capacity, which is smaller than the molten globule state, but was greater than t

Who reads Characterization of Acid-induced Unfolding Intermediates of Glucose/xylose Isomerase?

Author

S. A. Pawar; V. V. Deshpande

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Physical Sciences)