The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate.

@article{Aoki1992TheLN,
  title={The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate.},
  author={Takayoshi Aoki and Taketoshi Umeda and Yoshitaka Kako},
  journal={Journal of dairy science},
  year={1992},
  volume={75 4},
  pages={
          971-5
        }
}
Artificial casein micelles were formed with whole human casein at 20 mM calcium, 17 mM phosphate, and 10 mM citrate. The casein micelles disaggregated by 6 M urea were separated by high performance gel chromatography on a TSK-GEL G4000SW column into crosslinked and monomeric fractions. When the crosslinked casein fraction was analyzed by high performance ionexchange chromatography on a TSK-GEL DEAE-5PW column, a small peak, representing the 3-P component of human beta-casein, and distinct peaks… 

Effect of Alkaline Earth Metals on the Crosslinking of Casein by Micellar Calcium Phosphate

Abstract Artificial casein micelles were prepared by adding 20 to 30m M calcium, 17 to 22m M phosphate, and 10m M citrate to whole casein solutions. To casein micelles, 2.5 to 10m M magnesium,

A quantitative model of the bovine casein micelle: ion equilibria and calcium phosphate sequestration by individual caseins in bovine milk

An improved model of the partition of caseins and salts in milk is described in which all the phosphorylated residues in competent caseins act together to bind to and sequester the nanoclusters.

Determination of molecular weight of a purified fraction of colloidal calcium phosphate derived from the casein micelles of bovine milk.

Attempts to estimate the M(w) of the phosphopeptides associated with CCP using sodium dodecyl sulfate-PAGE were not successful, as they did not observe any peptide bands in these gels, presumably because of their low concentration in the isolated, unconcentrated fraction.

Effect of Modification of Amino Groups on Crosslinking of Casein by Micellar Calcium Phosphate

Abstract Bovine α s1 -CN was acetylated, succinylated, and citraconylated. Artificial casein micelles ( α s1 - κ -CN micelles) were prepared at a casein concentration of 2.5% with 20 to 50m M

Formation of Reconstituted Casein Micelles with Human β-Caseins and Bovine κ-Casein

Abstract Human β -casein (CN) is the major protein of the human milk casein fraction (∼80%) and exists in six calcium-sensitive forms, having zero to five organic phosphates per molecule. The major

Monomer characterization and studies of self-association of the major beta-casein of human milk.

The casein form that has four organic phosphoryl groups, beta-casein (CN)-4P, is the major constituent (approximately 35%) of the beta-CN fraction of human milk and should play an important role in

Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles

After extended tryptic hydrolysis of large bovine casein micelles, a mineral-rich peptide fraction was recovered by ultracentrifugation and the proportion of the phosphopeptides interacting with colloidal calcium phosphate was correlated with their relative content of phosphoserine residues.

Suspension of the Calcium-Sensitive Human β-Caseins by Human κ-Casein

The beta-casein (CN) fraction of human milk exists as a single protein entity phosphorylated at various levels from zero to five (beta-CN-0P to beta-CN-5P). Since the beta-CN fraction is precipitated

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Summary Artificial casein micelles were prepared at a casein concentration of 2·5% with 10–40 mM-Ca, 12–27 mM-phosphate and 10 mM-citrate and cross-linking of casein by colloidal Ca phosphate (CCP)

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