Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate.

  title={Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate.},
  author={Takayoshi Aoki and Nagisa Yamada and Isao Tomita and Yoshitaka Kako and Tsuneaki Imamura},
  journal={Biochimica et biophysica acta},
  volume={911 2},

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

The results indicate that at least three phosphate groups are needed for crosslinking of casein by colloidal calcium phosphate.

Incorporation of individual casein constituents into casein aggregates cross-linked by colloidal calcium phosphate in artificial casein micelles

  • T. Aoki
  • Chemistry
    Journal of Dairy Research
  • 1989
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)

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,

Dissociation during dialysis of casein aggregates cross-linked by colloidal calcium phosphate in bovine casein micelles

Summary Casein micelles separated by ultracentrifugation of raw skim milk were dispersed at a casein concentration of 2·5% in simulated milk ultrafiltrate and dialysed against 10 mM-imidazole buffer

Cleavage of the linkage between colloidal calcium phosphate and casein on heating milk at high temperature

Summary In order to examine the effect of heating on the changes in the linkage between colloidal Ca phosphate (CCP) and casein, high-performance gel chromatography of casein micelles disaggregated

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

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.

Preparation and characterization of micellar calcium phosphate-casein phosphopeptide complex.

It was confirmed by high-performance gel chromatographic analysis that the form of calcium phosphate in the MCP-CPP complex was similar to that of casein micelles, and this form was also separated from commercial rennet casein.



Effects of Chemical Phosphorylation of Bovine Casein Components on the Properties Related to Casein Micelle Formation

Bovine casein components (αsl-, β-, and κ-caseins) were chemically phosphorylated and the properties of the modified components were compared with those of the native to clarify the function of the

Composition and Properties of Submicellar Casein Complexes in Colloidal Phosphate-Free Skimmilk

Abstract Colloidal phosphate-free milks prepared from raw or heated (80C for 30min) skimmilk by adjustment to pH 4.9 or addition of ethylenediaminetetraacetate followed by dialysis were similar in

Sub-structure of synthetic casein micelles

It is shown that for the production of synthetic casein micelles with the same sub-structure as the natural ones it is necessary to add at least 2 other ions to the casein solution besides Ca2+: these are phosphate and citrate.

Review: Casein micelle structure; an examination of models.

  • C. Slattery
  • Chemistry, Medicine
    Journal of dairy science
  • 1976
The casein micelle system of bovine milk is unique in that protein aggregates of similar spherical shape but extreme variability of size are formed by the self-assembly of three major nonidentical subunits, which can be accounted for by only three models.

An improved method for the quantitative fractionation of casein mixtures using ion-exchange chromatography

The method uses ion-exchange chromatography at 4 °C on DEAE cellulose, Whatman DE52 in the presence of tris-chloride-urea buffer and a NaCl gradient to fractionate the alkylated casein mixtures and a micro-biuret technique to determine protein concentrations.

Purification and Some of the Properties of αs-Casein and κ-Casein

Summary α s -Casein and κ -casein have been freed of major contaminants, judged by starch-gel-urea electrophoresis. The α s -casein was prepared by a urea-sodium chloride procedure with a final

Preparation of κ-Casein by Gel Filtration

Abstract A procedure for the preparation of pure κ-casein by Sephadex gel filtration is described. Unreduced casein is filtered through a 2.5- by 95-cm column of Sephadex G-150 equilibrated with

Preparation of β-casein by a modified urea fractionation method

It has been shown by Hipp, Groves, Custer & McMeekin (1952) that the differential solubility in urea of the casein components of cow's milk can be utilized for preparative purposes. Fractionation is

Studies on a phosphoprotein phosphatase derived from beef spleen.