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Title of Journal: Amino Acids

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Abbravation: Amino Acids

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Springer Vienna

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DOI

10.1016/0002-9378(53)90213-0

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1438-2199

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Acidinduced unfolding of didecameric keyhole limp

Authors: Ankita Varshney Basir Ahmad Gulam Rabbani Vijay Kumar Savita Yadav Rizwan Hasan Khan
Publish Date: 2010/03/07
Volume: 39, Issue: 3, Pages: 899-910
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Abstract

Keyhole limpet hemocyanin KLH is widely used as an immune stimulant and hapten carrier derived from a marine mollusc Megathura crenulata To provide details of the stability and equilibrium of KLH different intermediate species were investigated with a series of biophysical techniques circular dichroism binding of hydrophobic dye 1anilino8naphthalene sulfonic acid acrylamideinduced fluorescence quenching thermal stability and dynamic light scattering KLH in its native state at pH 74 exists in the stable didecameric form with hydrodynamic radii R h of 2822 nm which is approximately equal to a molecular mass of 88 ± 06 MDa The experimental results demonstrated the presence of two structurally distinct species in the conformational transition of KLH under acidic conditions One species populates at pH 28 characterized as decameric 48 ± 02 MDa R h = 2202 nm molten globulelike state while the other accumulates at pH 12 and is characterized as a tetramer 24 ± 08 MDa R h = 1647 nm with more organized secondary and tertiary structures Our experimental manipulation of the oligomeric states of KLH has provided data that correlate well with the known oligomeric forms obtained from total KLH formed in vivo and extends our understanding of multimer formation by KLH The results are of particular interest in light of the important role of the mechanistic pathway of pHdependent structural changes of Hc stability in the biochemical and medical applications of these respiratory proteins

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