Heat-Induced Gelation of β-Lactoglobulin. 1. Time-Resolved Dynamic Light Scattering
Author:
Affiliation:
1. Department of Polymer Science and Engineering, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Inorganic Chemistry,Polymers and Plastics,Organic Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ma0003295
Reference35 articles.
1. Thermodynamic analysis of the monomer-dimer association of .beta.-lactoglobulin A at the isoelectric point
2. Proton relaxation rates of water in dilute solutions of β-lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self-associating globular protein
3. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
4. Calorimetric study of the heat and cold denaturation of .beta.-lactoglobulin
5. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins
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