Interaction Properties of Doubly Phosphorylated β-Casein, a Major Component of the Human Milk Caseins

Author:

Sood Satish M.,Chang Pat,Slattery Charles W.

Publisher

American Dairy Science Association

Subject

Genetics,Animal Science and Zoology,Food Science

Reference26 articles.

1. Extension of the fragment method to calculate amino acid Zwitterion and side chain partition coefficients;Abraham;Proteins Struct. Funct. Genet.,1987

2. Effect of bound phosphate on the calcium-binding ability and calcium dependent precipitability of human β-casein;Azuma;Agric. Biol. Chem.,1989

3. On the average hydrophobicity of proteins and the relation between it and protein structure;Bigelow;J. Theor. Biol.,1967

4. Structure and stability of casein micelles;Bloomfield;J. Dairy Sci.,1974

5. Binding of diffusible molecules by macromolecules: rapid measurement by rate of dialysis;Colowick;J. Biol. Chem.,1969

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