Chaperone activities of bovine and camel β-caseins: Importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation
| Autor: | Ali Akbar Saboury, Michèle Dalgalarrondo, Jean-Marc Chobert, Reza Yousefi, Ahmad Sharifzadeh, Abolfazl Barzegar, Parviz Norouzi, Thomas Haertlé, Amir Niasari-Naslaji, Mohammad Reza Ganjali, Mohammad Reza Ehsani, Ali Akbar Moosavi-Movahedi |
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| Přispěvatelé: | Institute of Biochemistry and Biophysics, Pawinskiego 5a, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), University of Tehran, Department of Clinical Sciences, Faculty of Veterinary Medicine |
| Rok vydání: | 2008 |
| Předmět: |
Camelus
Molecular Sequence Data BETA-CASEIN Biochemistry Micelle Anilino Naphthalenesulfonates Structural Biology [SDV.IDA]Life Sciences [q-bio]/Food engineering Animals [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering Amino Acid Sequence Horses Chaperone activity Molecular Biology Peptide sequence Micelles Alcohol dehydrogenase CHAPERONE HYDROPHOBICITY Dose-Response Relationship Drug Sequence Homology Amino Acid biology Alcohol Dehydrogenase Temperature Caseins Aggregation rate General Medicine AGGREGATION ALCOHOL DEHYDROGENASE (ADH) In vitro Liver Chaperone (protein) INTRINSICALLY UNSTRUCTURED PROTEINS (IUP) biology.protein Cattle Relevant information CHAPERON MOLECULAIRE Molecular Chaperones |
| Zdroj: | International Journal of Biological Macromolecules International Journal of Biological Macromolecules, Elsevier, 2008, 42 (4), pp.392-399. ⟨10.1016/j.ijbiomac.2008.01.008⟩ |
| ISSN: | 0141-8130 |
| Popis: | Beta-casein (beta-CN) showing properties of intrinsically unstructured proteins (IUP) displays many similarities with molecular chaperones and shows anti-aggregation activity in vitro. Chaperone activities of bovine and camel beta-CN were studied using alcohol dehydrogenase (ADH) as a substrate. To obtain an adequate relevant information about the chaperone capacities of studied caseins, three different physical parameters including chaperone constant (k(c), microM(-1)), thermal aggregation constant (k(T), degrees C(-1)) and aggregation rate constant (k(t), min(-1)) were measured. Bovine beta-CN displays greater chaperone activity than camel beta-CN. Fluorescence studies of 8-anilino-1-naphthalenesulfonic acid (ANS) binding demonstrated that bovine beta-CN is doted with larger effective hydrophobic surfaces at all studied temperatures than camel beta-CN. Greater relative hydrophobicity of bovine beta-CN than camel beta-CN may be a factor responsible for stronger interactions of bovine beta-CN with the aggregation-prone pre denatured molecular species of the substrate ADH, which resulted in greater chaperone activity of bovine beta-CN. |
| Databáze: | OpenAIRE |
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