Literature DB >> 11902669

Evaluation of hydrophobicity versus chaperonelike activity of bovine alphaA- and alphaB-crystallin.

Jaya Bhattacharyya1, V Srinivas, K Krishna Sharma.   

Abstract

Calf lens alphaA-crystallin isolated by reversed-phase HPLC demonstrates a slightly more hydrophobic profile than alphaB-crystallin. Fluorescent probes in addition to bis-ANS, like cis-parinaric acid (PA) and pyrene, show higher quantum yields or Ham ratios when bound to alphaA-crystallin than to alphaB-crystallin at room temperature. Bis-ANS binding to both alphaA- and alphaB-crystallin decreases with increase in temperature. At room temperature, the chaperone-like activity of alphaA-crystallin is lower than that of alphaB-crystallin whereas at higher temperatures, alphaA-crystallin shows significantly higher protection against aggregation of substrate proteins compared to alphaB-crystallin. Therefore, calf lens alphaA-crystallin is more hydrophobic than alphaB-crystallin and chaperone-like activity of alpha-crystallin subunits is not quantitatively related to their hydrophobicity.

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Year:  2002        PMID： 11902669     DOI： 10.1023/a:1014187300930

Source DB:  PubMed          Journal:  J Protein Chem        ISSN： 0277-8033


  9 in total

1.  The SC3 hydrophobin self-assembles into a membrane with distinct mass transfer properties.

Authors:  X Wang; Fuxin Shi; H A B Wösten; H Hektor; B Poolman; G T Robillard
Journal:  Biophys J       Date:  2005-03-04       Impact factor: 4.033

2.  Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.

Authors:  Ram H Nagaraj; Rooban B Nahomi; Shilpa Shanthakumar; Mikhail Linetsky; Smitha Padmanabha; Nagarekha Pasupuleti; Benlian Wang; Puttur Santhoshkumar; Alok Kumar Panda; Ashis Biswas
Journal:  Biochim Biophys Acta       Date:  2011-11-18

3.  Succinylation Is a Gain-of-Function Modification in Human Lens αB-Crystallin.

Authors:  Sandip K Nandi; Stefan Rakete; Rooban B Nahomi; Cole Michel; Alexandra Dunbar; Kristofer S Fritz; Ram H Nagaraj
Journal:  Biochemistry       Date:  2019-02-20       Impact factor: 3.162

4.  Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.

Authors:  Ashis Biswas; Antonia Miller; Tomoko Oya-Ito; Puttur Santhoshkumar; Manjunatha Bhat; Ram H Nagaraj
Journal:  Biochemistry       Date:  2006-04-11       Impact factor: 3.162

5.  Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.

Authors:  Puttur Santhoshkumar; K Krishna Sharma
Journal:  Protein Sci       Date:  2006-11       Impact factor: 6.725

6.  Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays.

Authors:  M Satish Kumar; P Yadagiri Reddy; P Anil Kumar; Ira Surolia; G Bhanuprakash Reddy
Journal:  Biochem J       Date:  2004-04-15       Impact factor: 3.857

7.  Paradoxical acceleration of dithiothreitol-induced aggregation of insulin in the presence of a chaperone.

Authors:  Zoya Bumagina; Bella Gurvits; Natalya Artemova; Konstantin Muranov; Boris Kurganov
Journal:  Int J Mol Sci       Date:  2010-11-15       Impact factor: 5.923

8.  Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.

Authors:  Ram H Nagaraj; Alok Kumar Panda; Shilpa Shanthakumar; Puttur Santhoshkumar; NagaRekha Pasupuleti; Benlian Wang; Ashis Biswas
Journal:  PLoS One       Date:  2012-01-17       Impact factor: 3.240

9.  Comparison of effect of gamma ray irradiation on wild-type and N-terminal mutants of αA-crystallin.

Authors:  Srinivasagan Ramkumar; Noriko Fujii; Norihiko Fujii; Bency Thankappan; Hiroaki Sakaue; Kim Ingu; Kalimuthusamy Natarajaseenivasan; Kumarasamy Anbarasu
Journal:  Mol Vis       Date:  2014-07-07       Impact factor: 2.367
  9 in total

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