Caseinomacropeptide self-association is dependent on whether the peptide is free or restricted in kappa-casein.

  title={Caseinomacropeptide self-association is dependent on whether the peptide is free or restricted in kappa-casein.},
  author={T. L. Mikkelsen and Hanne Fr{\o}kiaer and Christopher Topp and Francesco Bonomi and Stefania Iametti and Gianluca Picariello and Pasquale Ferranti and Vibeke Barkholt},
  journal={Journal of dairy science},
  volume={88 12},
There is a general agreement that the experimentally determined molecular weight (MW) of caseinomacropeptide (CMP) is greater than the theoretical MW. Some studies suggest that this is due to a pH-dependent aggregation of monomeric CMP. How this aggregation is influenced by pH is not understood. This study was carried out to study the nature of CMP aggregates and to clarify which conditions affect aggregation of CMP. The apparent MW of CMP at different pH values was determined using size… 
The objective of this work was to review the isolation and purification methods of glycomacropeptide (gmp). This peptide is formed during enzymatic coagulation of milk, using chymosin. Aspects such


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Some association properties of bovine SH-k-casein
Comparative study of methods for the isolation and purification of bovine κ-casein and its hydrolysis by chymosin
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Purification of κ‐Casien Glycomacropeptide from Sweet Whey with Undetectable Level of Phenylalanine
The purified GMP was of high purity, with its amino acid composition showing undetectable levels of phenylalanine, tyrosine and arginine, the amino acids that do not occur in bovine GMP.
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