Influence of the Ionic Strength on the Structure of Heat-Set Globular Protein Gels at pH 7. Ovalbumin
Authors:
- 14 October 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Macromolecules
- Vol. 37 (23) , 8709-8714
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Influence of the Ionic Strength on the Structure of Heat-Set Globular Protein Gels at pH 7. β-LactoglobulinMacromolecules, 2004
- Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7International Journal of Biological Macromolecules, 2004
- Light Scattering Study of Heat-Induced Aggregation and Gelation of OvalbuminMacromolecules, 2002
- Globular protein gelationCurrent Opinion in Colloid & Interface Science, 2000
- Isolation of hen egg white lysozyme, ovotransferrin and ovalbumin, using a quaternary ammonium bound to a highly crosslinked agarose matrixJournal of Chromatography B: Biomedical Sciences and Applications, 1995
- Dynamic light scattering of aqueous solutions of linear aggregates induced by thermal denaturation of ovalbuminBiopolymers, 1993
- Crystal structure of uncleaved ovalbumin at 1·95 Å resolutionJournal of Molecular Biology, 1991
- Characterization of linear polymers induced by thermal denaturation of ovalbuminFood Hydrocolloids, 1989