A method for modification of carboxyl groups in proteins: Its application to the association of bovine β-lactoglobulin A
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference15 articles.
1. Milk Proteins
2. Optical rotatory dispersion and sedimentation in the study of association-dissociation: Bovine β-lactoglobulins near pH5
3. Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22
4. The pH dependence of the association of β-lactoglobulin
5. Structural and Genetic Implications of the Physical and Chemical Differences Between β-Lactoglobulins A and B
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3. Improvement of the MS/MS Fragment Ion Coverage of Acidic Residue-Containing Peptides by Amidation with 15N-Substituted Amine;Analytical Chemistry;2004-09-08
4. β-Lactoglobulin;Advanced Dairy Chemistry—1 Proteins;2003
5. [15] Amidation of basic carboxyl groups of hemoglobin;Hemoglobins Part B: Biochemical and Analytical Methods;1994
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