Casein spleen

Milk acid phosphatase has been purified to homogeneity by various forms of chromaotgraphy, including affinity chromatography purification up to 40 000-fold has been claimed. The enzyme shows broad specificity on phosphate esters, including the phosphoseryl residues of casein. It has a molecular mass of about 42 kDa and an isoelectric point of 7.9. Many forms of inorganic phosphate are competitive inhibitors, while fluoride is a powerful non-competitive inhibitor. The enzyme is a glycoprotein and its amino acid composition is known. Milk acid phosphatase shows some similarity to the phosphoprotein phosphatase of spleen but differs from it in a number of characteristics. 

Oral administration of the hot-water extracts in mice suppressed the immunoglobulin E (IgE) production against casein antigen, accompanied by increased IFNy and IL-12 mRNA expression [26], Oral administration of the extracts enhanced Thl response to casein in the spleen of casein-immunized mice. The hot-water extracts may be useful for the pre-... 

Otani, H. and Hata, I. 1995. Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer s patch cells by bovine milk caseins and their digests. J. Dairy Res. 62, 339-348. 

G5. Glomset, J. A., The further purification and properties of a phosphatase from spleen able to hydrolyze completely the phosphorus of L. Casein. Biochim. Biophys. Acta 32, 349-357 (1959). 

In a recent communication Sundararajan and Sarma report that a phosphoprotein phosphatase from rat spleen dephosphorylates a-, /3-, and unfractionated casein (90). Since these authors state that their enzyme differs in its action from that of a phosphomonoesterase, their results are in accord with the occurrence of a variety of phosphorus bonds in proteins. In this connection it should be noted that intestinal phosphatase used in our work at pH 9.0 also liberates all of the a-casein phosphorus (72). As discussed earlier, although this enzyme at pH 6.0 hydrolyzes —N—P—... 

Figure 9 RT-PCR analysis of cytokine mRNA expression in the spleens of DBA/2 mice immunized with casein/CKA. Total RNA was extracted from pooled spleens of S DHA/2 mice or CVE-administercd mice 3 weeks after immunized using RNAzol and reverse-transcribed, and the cDNA concentration was adjusted by co-amplification of two fold serially diluted cDNA and constant amounts of control plasmid pMCQ with [5-actin specific primers. Cytokine expression patterns of IL-12, IFNy, IL-6, and 11.-10 were determined by PCR using murine cytokine-specific primers. The PCR products were separated in 2 % agarose gel and visualized by ethidium bromide staining. Relative quantification of the amounts of the RT-PCR products was performed using a Computing Densitometer and NIH Image software,...

In order to confirm the effects of oral administration of CVE on the IL-12 and IFNy mRNA expressions in the spleens of mice immunized with casein/CFA, we compared the expression of cytokine genes in the spleens of untreated and CVE-treated mice after immunization with casein/CFA. Total RNA was extracted from the spleens 3 weeks after immunization. The levels of IL-12 and IFNy were augmented in the... 

Here, we showed that the production of casein-specific IgE Ab in mice immunized with casein/CFA was suppressed by oral administration of CVE, and that the production of casein-specific IgG2a levels was enhanced by oral administration of CVE, whereas the expressions of IL-12 and IFNy mRNAs were increased in the spleens of mice after immunization with casein/CFA. These results suggested that CVE may be useful as a therapeutic or prophylactic agent to control allergy accompanied by the elevation of allergen-specific IgE Abs. 

Storage Store nutrients Casein stores protein in milk. Ferritin stores iron in the spleen and liver. 

Concentration of taurine (a) and activity of hypotaurine oxydase (b) in kidney and spleen of rats fed on a 18% casein diet (A) and on a 60% casein diet (B). 

From these figures it appears that, whatever the diet, the concentration of taurine was the same in the spleen whereas it was increased in the kidney of rats fed on the 60% casein diet, which is in keeping with our previous observations H. Furthermore the formation of taurine from hypotaurine remained approximatively the same whatever the diet in the spleen while a clear increase was observed in the kidney of the 60% casein fed rats. 

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