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Water Interactions in Bovine Casein: 2H NMR Relaxation and Small-Angle X-Ray Scattering Studies

  • Helmut Pessen
  • Thomas F. Kumosinski
  • Harold M. FarrellJr.
Part of the Basic Life Sciences book series (BLSC, volume 56)

Abstract

Whole casein occurs in bovine milk as a colloidal calcium-containing protein complex, commonly called the casein micelle. Removal of calcium is thought to result in the dissociation of this micellar structure into non-colloidal protein complexes called submicelles (Farrell, 1988). These submicelles consist of four proteins, αs1 -, αs2 -, β-, and κ-casein, in the approximate ratios of 4:1:4:1 (Davies and Law, 1980). All are phosphorylated to various extents, have an average monomer molecular weight of 23,300, and are considered to have little or no secondary structure (Farrell and Thompson, 1988). The major casein fraction, αs1, a single-chain polypeptide of 199 amino acid residues, contains 8 phosphoserine residues (Eigel et al., 1984) and a large number of hydrophobic residues; the weight-average number of phosphate groups is 6.6 per monomer.

Keywords

Casein Micelle Trap Water Micellar Structure Transverse Relaxation Rate SAXS Data 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Helmut Pessen
    • 1
  • Thomas F. Kumosinski
  • Harold M. FarrellJr.
  1. 1.ERRCUSDAPhiladelphiaUSA

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