期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 45, 期 3, 页码 248-254出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2009.05.008
关键词
Ficin; Protein folding; Molten globule; Acid-unfolding; Cysteine protease
资金
- Council of Scientific and Industrial Research, Government of India, New Delhi, India
Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CID, intrinsic fluorescence and ANS binding studies demonstrate that ficin exhibits the characteristic properties of molten globule at acidic conditions between pH 1.4 and 2.0. Ficin at pH 1.4 retained about similar to 74% secondary structure with a substantial loss of tertiary structure. The acid-induced state was found to have a compact shape as measured by Stokes radius on size exclusion chromatography. (C) 2009 Elsevier B.V. All rights reserved.
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