Literature DB >> 19482042

Characterization of acid-induced molten globule like state of ficin.

K B Devaraj1, Parigi Ramesh Kumar, V Prakash.   

Abstract

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 CD, 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 approximately 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.

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Year:  2009        PMID: 19482042     DOI: 10.1016/j.ijbiomac.2009.05.008

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  3 in total

1.  Metastability of papain and the molecular mechanism for its sequential acid-denaturation.

Authors:  Rosa Eréndira Fosado-Quiroz; Arturo Rojo-Domínguez
Journal:  Protein J       Date:  2011-03       Impact factor: 2.371

2.  1-Anilino-8-naphthalene sulfonate (ANS) is not a desirable probe for determining the molten globule state of chymopapain.

Authors:  Atiyatul Qadeer; Gulam Rabbani; Nida Zaidi; Ejaz Ahmad; Javed M Khan; Rizwan H Khan
Journal:  PLoS One       Date:  2012-11-29       Impact factor: 3.240

3.  Unfolding studies of the cysteine protease baupain, a papain-like enzyme from leaves of Bauhinia forficata: effect of pH, guanidine hydrochloride and temperature.

Authors:  Rosemeire A Silva-Lucca; Sheila S Andrade; Rodrigo Silva Ferreira; Misako U Sampaio; Maria Luiza V Oliva
Journal:  Molecules       Date:  2013-12-24       Impact factor: 4.411

  3 in total

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