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PubMed2001

Mass spectrometry-based procedure for the identification of ovine casein heterogeneity.

The efficiency of reversed-phase HPLC, capillary electrophoresis (CE), PAGE and isoelectric focusing with immunoblotting in separating ovine caseins has been evaluated. The assessment was carried out by employing electrospray ionization-mass spectrometry (ESI-MS) and matrix-assisted laser desorption ionization-time of flight as reference tools for identifying protein components. Ovine casein was fractionated by HTPC into four major peaks. With ESI-MS, each peak contained components belonging to only one of the four casein families. On-line liquid chromatography-ESI-MS allowed us to determine each fraction's composition by detecting thirteen alphas1-, eleven alphas2-, seven beta-, and three kappa-casein (CN) components. The alphas1-CN and alphas2-CN consisted of eight and two protein chains respectively of lengths differing through the deletion of one or more peptide sequences; they were also discretely phosphorylated as kappa-CN and beta-CN. By CE at pH 2.5, each casein fraction was as heterogeneous as that resulting from ESI-MS for the single HPLC-derived fractions. The separation of alphas1-CN and alphas2-CN proved to be excellent, with the exception of a co-migration of kappa0-CN with a minor alphas1-CN component and of a glycosylated kappa-CN for with low-phosphorylated = alphas1-CN and beta-CN components. Dephosphorylation of whole casein was used to reduce the heterogeneity of the native fractions and by applying currently used analytical techniques it was possible to visualize the protein moiety difference along the CE profile. CE, HPLC, and immunoblotting were all equally capable of effecting an accurate separation of the four dephosphorylated casein families. The spectra obtained by ESI-MS directly on dephosphorylated whole ovine casein samples contained the signals of the four casein families and the relative alphas1-CN variants, the non-allelic alphas1-CN and alphas2-CN forms, dimeric kappa-CN and other newly formed peptides. We suggest using this procedure for rapid characterization of whole casein.

Animals↗
PubMed1985

Quantification of beta-casein in human milk.

A method is described for preparing immunologically homogeneous human milk beta-casein, against which monospecific rabbit antiserum was prepared. The antiserum was used to quantify beta-casein, the major human casein, by rocket immunoelectrophoresis in individual milk samples. However, it was found that in most samples beta-casein occurred together with degradation products originating from its proteolysis by plasmin. Immunological quantification of human beta-casein, treated with plasmin for various time periods, showed that rocket height was not affected by proteolysis up to degradation states clearly more advanced than those observed in all samples of fresh human milk tested. Assays of 150 individual milk samples from 80 women, covering a lactation period of up to 730 d, gave an average concentration of beta-casein (native + degraded) of 4.67 +/- 0.89 standard deviation (g/l); extremes at 2.1 and 7.3 g/l did not vary significantly during the period under study. Comparison of this average value with an accepted casein content of 4.4 g/l (Macy & Kelly, 1961) showed that the casein content of human milk is underestimated when obtained by N determinations on milk and on its supernatants at pH 4.6 (whey). Caseins other than beta-casein occurred only in minute amounts, if at all.

Amino Acids↗
PubMed1995

Changes in casein composition of goats' milk during the course of lactation: physiological inferences and technological implications.

Five British Saanen goats were milk sampled during the first 39 weeks of lactation to determine changes in casein composition. Caseins were separated by anion- and cation-exchange FPLC to determine the relative amounts of the individual caseins. Acid, alkaline and SDS-PAGE were used to determine possible genetic polymorphisms and observe any lactational changes. Total casein nitrogen was determined using a micro-Kjeldahl method and this allowed the concentrations of individual caseins to be calculated. The milk of one animal, which had the deduced genotype alpha s1-CnAB, showed higher concentrations of both total and alpha s1-casein. The remainder of the group were either heterozygous alpha s1-CnBE or, more probably, homozygous alpha s1-CnE and produced milk of a generally lower protein concentration. Both FPLC and PAGE results showed that the relative amounts and concentrations of alpha s2-casein decreased with stage of lactation, consistent with its susceptibility to proteolysis. The relative amounts of the breakdown products of plasmin attack on beta-casein, gamma-caseins, were highly negatively correlated with milk yield (r = -0.942, P < 0.001) in the declining phase of lactation, reflecting the gradual involution of the gland at this time. The relative amount of kappa-casein increased by approximately 50% after peak lactation and its concentration almost doubled near the end of lactation. These compositional changes may alter the processing qualities of goats' milk in relation to cheese production.

Animals↗
PubMed2003

Heat-induced interactions of beta-lactoglobulin A and kappa-casein B in a model system.

The interaction of kappa-casein and beta-lactoglobulin is fundamental to all heat-induced modifications of milk product functionality, such as the heat stability of concentrated milks. Purified native kappa-casein B and beta-Ig A solutions were heated at 80 degrees C at pH 6.7 separately and in a mixture. The circular dichroism spectra in the near UV indicated irreversible changes in the disulphide bonding patterns involving both proteins. Alkaline- and SDS-PAGE of heated samples showed that, in the presence of kappa-casein, less beta-Ig was converted into beta-Ig polymers and the rate of loss of native beta-Ig was greater. When kappa-casein was added to previously heated beta-Ig and the mixture was heated, the kappa-casein reacted with the heat-induced beta-Ig polymers more readily than with the beta-Ig native monomers. The formation of beta-Ig dimers, trimers etc. was diminished. It was concluded that, when beta-Ig and kappa-casein were heated together, beta-Ig formed thiol-exposed monomers, which reacted with each other or with the native kappa-casein depending on the relative concentrations of beta-Ig and kappa-casein. The products of these reactions included some disulphide-bonded 1:1 beta-Ig:kappa-casein complexes, some monomer kappa-casein and a range of large aggregates held together by either or both disulphide bonds and hydrophobic association.

Caseins↗
PubMedDate not supplied

Electrosorption of pectin onto casein micelles.

Pectin, a polysaccharide derived from plant cells of fruit, is commonly used as stabilizer in acidified milk drinks. To gain a better understanding of the way that pectin stabilizes these drinks, we studied the adsorption and layer thickness of pectin on casein micelles in skim milk dispersions. Dynamic light scattering was used to measure the layer thickness of adsorbed pectin onto casein micelles in situ during acidification. The results indicate that the adsorption of pectin onto casein micelles is multilayered and takes place at and below pH 5.0. Renneting, i.e., cleaving-off kappa-casein from the casein micelles, did not alter the adsorption pH. It did, however, show that pectin arrests the rennet-induced flocculation of casein micelles below pH 5.0. From the findings we concluded the attachment of pectin onto casein micelles is driven by electrosorption. Adsorption measurements confirmed the multilayered nature of the adsorption of pectin onto casein micelles. Both the adsorbed amount and the layer thickness increased with decreasing pH in the relevant range 3.5-5.0. The phase behavior of a casein micelles/pectin mixture was determined and could be explained in terms of thermodynamic incompatibility being relevant above pH 5.0 and adsorption, leading to either stabilization and bridging, being relevant below pH 5.0. The results confirm that electrosorption is the driving force for the adsorption of pectin onto casein micelles.

Adsorption↗
PubMed2003

Effect of pH on the association of denatured whey proteins with casein micelles in heated reconstituted skim milk.

Skim milk was adjusted to pH values between 6.5 and 6.7 and heated (80, 90, and 100 degrees C) for up to 60 min. Changes in casein micelle size, level of whey protein denaturation, and level of whey protein association with the micelles were monitored for each milk sample. Changes in casein micelle size were markedly affected by the pH at heating. At low pH (6.5-6.55), the casein micelle size increased markedly during the early stages of heating, and the size plateaued on prolonged heating. The maximum increase in size was approximately 30-35 nm. In contrast, at high pH (6.7), much smaller changes in size were observed on heating and the maximum increase in size was only approximately 10 nm. An intermediate behavior was observed at pH values between these two extremes. The rate of denaturation of the major whey proteins, alpha-lactalbumin and beta-lactoglobulin, was essentially unaffected by the pH at heating for the small pH changes involved in this study, and the changes in casein micelle size were poorly related to the level of whey protein denaturation. In contrast, the level of denatured whey proteins associating with the micelles was markedly dependent on the pH at heating, with high levels of association at pH 6.5-6.55 and low levels of association at pH 6.7. Changes in casein micelle size were related to the levels of denatured whey proteins that were associated with the casein micelles, although there was a small deviation from linearity at low levels of association (<15%). Further studies on reconstituted and fresh milk samples at smaller pH steps confirmed that the association of whey proteins with the casein micelles was markedly affected by the pH at heating. These results indicate that the changes in casein micelle size induced by the heat treatment of skim milk were a consequence of the whey proteins associating with the casein micelles and that the level of association was markedly influenced by small pH changes of the milk. It was not possible to determine whether the association itself influenced the casein micelle size or whether parallel reactions involving micellar aggregation caused the increase in micelle size as whey protein association progressed.

Animals↗
PubMed2004

Redox-related cytotoxic responses to different casein glycation products in Caco-2 and int-407 cells.

Sugar-casein glycation products (GPs) were generated by Maillard reaction (MR) with different monosaccharide sources [e.g., glucose (Glc), fructose (Fru), and ribose (Rib)] and prolonged heating (e.g., 27 days at 55 degrees C) to produce Maillard reaction products (MRPs) that varied in opponent (L, a, b) color measurement and changes in pH, available lysine, and amino-sugar ratio. Theses results signified different rates of three sugar and casein glycation. Sugar-casein GPs from aldohexose, ketohexose, and aldopentose sugar sources were recovered on day 18 of heating and compared for bioactive properties using human embryonic intestinal cell (Int-407) and adenocarcinoma cell (Caco-2) lines. Glu- and Fru-casein GPs produced significant (p < 0.05) decreases in antioxidant superoxide dismutase (SOD), glutathione peroxidase, and glutathione reductase enzyme activities in the Int-407 cell line, whereas no effect on antioxidant enzymes was obtained from Rib-casein GP. Moreover, the Caco-2 cell antioxidant enzyme status was not affected by the presence of sugar-casein GPs, regardless of sugar source. The reduction in antioxidant enzyme activity of Int-407 cells by Glu and Fru- casein GPs corresponded to a significant (p < 0.05) reduction in Int-407 cell viability. In contrast, no change in Caco-2 cell viability was observed with sugar-casein GP. This finding demonstrates that the noted variable cytotoxic, sugar specific effects of casein GP were related to reductions in critical antioxidant enzyme activities. Moreover, the source of intestinal cell line was an important factor to show the effect of sugar-casein GPs on redox-related cytotoxicity.

Antioxidants↗
PubMed2005

Reversible precipitation of casein micelles with a cationic hydroxyethylcellulose.

The cationic hydroxyethylcellulose Polyquaternium 10 (PQ10) was found to produce a dose-dependent destabilization of casein micelles from whole or skim milk without affecting the stability of most of the whey proteins. The anionic phosphate residues on caseins were not determinant in the observed interaction since the destabilization was also observed with dephosphorylated caseins to the same extent. However, the precipitation process was completely inhibited by rising NaCl concentration, indicating an important role of electrostatic interactions. Furthermore, the addition of 150 mM NaCl solubilized preformed PQ10-casein complexes, rendering a stable casein suspension without a disruption of the internal micellar structure as determined by dynamic light scattering. This casein preparation was found to contain most of the Ca2+ and only 10% of the lactose originally present in milk and remained as a stable suspension for at least 4 months at 4 degrees C. The final concentration of PQ10 determined both the size of the casein-polymer aggregates and the amount of milkfat that coprecipitates. The presence of PQ10 in the aggregates did not inhibit the activity of rennet or gastrointestinal proteases and lipases, nor did it affect the growth of several fermentative bacteria. The cationic cellulose PQ10 may cause a reversible electrostatic precipitation of casein micelles without disrupting their internal structure. The reversibility of the interaction described opens the possibility of using this cationic polysaccharide to concentrate and resuspend casein micelles from whole or skim milk in the production of new fiber-enriched lactose-reduced calcium-caseinate dairy products.

Animals↗
PubMed2005

Effects of added sodium caseinate on the formation of particles in heated milk.

The effects of heat at temperatures in the range of 80-90 degrees C on mixtures of reconstituted skim milk powder (RSMP) and sodium caseinate have been determined. In the absence of caseinate, the action of heat on RSMP produces soluble complexes of whey proteins and kappa-casein, as well as complexes of whey protein with the casein micelles. When sodium caseinate was added to RSMP at levels of 0.5 and 1.0%, the denaturation of the whey protein and the production of the soluble complexes in the serum were hardly affected, either in rate or in amount. However, during the heating, the caseinate disappeared from the serum. Further studies on model mixtures of the different components showed that it was probable that the bulk of the caseinate associated with the casein micelles during heating, probably by binding inside the surface layer of kappa-casein, because no increase in the diameters of the casein micelles could be observed.

Animals↗
PubMed1999

Overphosphorylation of milk caseins by a recombinant protein kinase CK2 catalytic subunit.

Milk caseins have been phosphorylated by a recombinant protein kinase CK2 catalytic subunit from Schizosaccharomyces pombe (rspCK2alpha). Phosphate incorporation stoechiometries into purified caseins and into native phosphocaseinate, a substrate exhibiting a micellar-like structure, were determined. We incorporated 2.01 mol of P/mol of alpha-casein, 6.46 mol of P/mol of beta-casein, up to 0. 29 mol of P/mol of kappa-casein in 4 h, and more than 1.36 mol of P/mol of casein into phosphocaseinate under optimized conditions. Phosphocaseinate was sequentially phosphorylated; beta-caseins being labeled at first; alpha-caseins being labeled later; and to a lower extend, kappa-caseins were the last to be phosphorylated. The solubility of phosphocaseinate micelles increased by 1.34 from 65 to 87%, and its rennetting time was increased 2.88 times. These results are discussed in terms of plausible structural organization of caseins micelles and the effect of phosphorylation on their structure.

Animals↗
PubMed1982

Extensive destruction of newly synthesized casein in mammary explants in organ culture.

1. Explants of mammary glands of mid-pregnant rabbits that had been cultured for 18h in the presence of insulin, prolactin and cortisol were incubated at 37 degrees C for 2h in Medium 199 containing l-[4,5-(3)H]leucine. After a wash procedure at 4 degrees C, explants were re-incubated at 37 degrees C in fresh medium and the radioactivity of casein polypeptides isolated by isoelectric focusing (at pH 4.6) was followed with time. Casein radioactivity rose during the first hour of re-incubation, but fell markedly during the subsequent hour. 2. Loss of radioactivity represented casein degradation, since less than 10% of newly synthesized casein was found in the incubation medium. 3. Such a loss of radioactivity was not due solely to hydrolysis of signal peptides, since similar results were obtained when l-[5-(3)H]proline, which is not part of casein signal peptides, was the radiolabelled precursor. 4. A dual-isotope experiment using l-[U-(14)C]proline and N-[(3)H]acetyl-d-mannosamine gave similar profiles of radioactivity loss from isoelectrically focused casein, indicating that degradation of mature casein was occurring. 5. Analysis of total pellet and particle-free-supernatant fractions prepared by centrifugation of explant homogenates at 115000g(av.) for 1h did not show loss of radioactivity on re-incubation. Total pellet-protein radioactivity remained constant, whereas total soluble-protein radioactivity increased during the 2h re-incubation period. 6. Radioactivity in a specific particle-free-supernatant polypeptide, the subunit of fatty acid synthetase, mimicked that of the total soluble protein. 7. Addition of cycloheximide (20mug/ml) during the re-incubation period completely blocked the incorporation of radioactivity from l-[5-(3)H]proline into casein and the subsequent fall, indicating that observations were being made on newly synthesized casein. 8. Addition of chloroquine (50mum) did not prevent the increase in radioactivity from l-[5-(3)H]proline into casein during the first hour of re-incubation, but did prevent the loss of radioactivity in the second hour. 9. The intracellular degradation of a newly synthesized milk protein is discussed in relation to the known intracellular degradation of other secretory polypeptides.

Animals↗
PubMed1984

Identification and subsequent phosphorylation of sequestered partially processed caseins in the lactating guinea-pig mammary gland.

Golgi and endoplasmic-reticulum fractions were prepared from the lactating guinea-pig mammary gland. The endoplasmic-reticulum fraction was highly active in the processing and sequestration of milk-protein primary translation products. Explants from the lactating gland in organ culture were used to identify milk-protein intermediates present in the secretory pathway, and the timing of the events leading to their post-translational modification. With [35S]methionine, the milk proteins labelled after a short pulse (3 min) were represented by the partially processed (but not phosphorylated) caseins and alpha-lactalbumin sequestered within membrane-bound vesicles. After a 30 min labelling period, higher-Mr caseins with electrophoretic mobilities identical with those of the phosphorylated caseins isolated from milk were identified in the incubation medium, and sequestered within membrane-bound vesicles. Pulse-chase experiments established a precursor-product relationship between these forms. Secretion is apparent approx. 30 min after sequestration. Caseins are highly phosphorylated; removal of the phosphate residues with acid phosphatase results in proteins with increased electrophoretic mobility, similar to those of the partially processed early casein intermediates found sequestered in explants after a 3 min pulse with [35S]methionine, and those sequestered within microsomal membranes after mRNA-directed cell-free protein synthesis. A comparison of the proteins labelled during both short (5 min) and long (30 min) pulses with [35S]methionine and [32P]Pi shows that, in contrast with the 35S-labelled caseins, those labelled with [32P]Pi exhibit only electrophoretic mobilities identical with those of the mature caseins isolated from milk and those identified after long labelling periods with [35S]methionine. No phosphorylated early intermediate forms of caseins were identified. We conclude that the synthesis and post-translational modification of guinea-pig caseins occurs in two stages, (i) an early event involving synthesis and sequestration within the endoplasmic reticulum, an event that involves signal-peptide removal, followed (ii) 10-20 min later by phosphorylation at a different point in the secretory pathway, probably in the Golgi complex. Secretion of the phosphorylated caseins occurs 10-20 min later.

Animals↗
PubMed1995

Expression analysis of the individual bovine beta-, alpha s2- and kappa-casein genes in transgenic mice.

To identify cis-acting regulatory elements involved in the regulation of expression of the casein genes, the bovine beta-, alpha s2- and kappa-casein genes were isolated from cosmid libraries and introduced into the murine germline. Bovine casein expression was analysed at the RNA and protein level. The bovine beta-casein gene, including 16 kb of 5'- and 8 kb of 3'-flanking region, appeared to be expressed in all 12 transgenic mouse lines analysed. In 50% of these lines expression levels in milk exceeded 1 mg/ml. Three lines displayed expression levels comparable with or well above (20 mg/ml) the beta-casein levels in bovine milk. Transgene expression was restricted to the mammary gland. Strong induction of expression occurred at parturition and thus resembled the bovine rather than the murine pattern. In spite of this high-level tissue-specific and developmentally regulated expression, beta-casein expression levels were integration-site-dependent, suggesting that not all elements involved in regulation of expression were included in this beta-casein clone. Neither the bovine alpha s2- nor the kappa-casein gene, including 8 kb and 5 kb of 5'- and 1.5 kb and 19 kb of 3'-flanking sequences respectively, were properly expressed in transgenic mice. However, they were transcribed in stably transfected mouse mammary epithelial cells. This indicates that regulatory elements required for high-level, mammary gland-specific expression are not present in the alpha s2- and kappa-casein clones used in this study and are probably located elsewhere in the casein gene locus.

Animals↗
PubMed1985

The importance of the non-protein components of the diet in the plasma cholesterol response of rabbits to casein.

To characterize the hypercholesterolaemic effect of casein further, four groups of young male rabbits in two separate experiments were placed on cholesterol-free semi-purified diets for 12 weeks. The diets were similar in composition, with either casein or soya-bean-protein isolate providing the protein source (250 g/kg). In two of these diets the salt mix was reduced by 45% (normally 40 g/kg) and replaced by potassium bicarbonate. Growth was unaffected by these alterations in dietary salts except for one group given the soya-bean-reduced-salts diet. The mean concentrations of plasma cholesterol were significantly higher in all casein-fed groups as compared with their soya-bean-fed counterparts but the response was much greater in those given the casein-reduced-salts diet. Contrary to expectations, analysis of the diets showed the zinc and copper concentrations of the casein diets to be less than those of the soya-bean diets. This was due to the greater concentrations of Cu (threefold) and Zn (twofold) in the soya-bean-protein isolate compared with casein. The mean concentration of Zn in fur was significantly decreased in casein-fed rabbits and these animals also excreted less Zn but more Cu in their urine than those given the casein-reduced-salts diet. The rabbits given the casein diet with the least salt mix showed the greatest degree of hypercholesterolaemia, suggesting an interaction between trace elements and the casein effect.

Animals↗
PubMed1986

The nitrogen and energy metabolism of lactating cows given abomasal infusions of casein.

1. Four cows in early lactation were given continuous infusion into the abomasum of 0, 200, 400 or 600 g lactic casein/d according to a Latin-square design. Each period was of 14 d and the Latin square was followed by 7 d in which an infusion of 800 g glucose/d was given. The basal diet was given at a level which provided sufficient nitrogen and energy for 10 kg milk yield/d. 2. Infusion of casein resulted in significant increases in milk yield, milk N yield and milk energy yield; milk N increased progressively but milk energy reached a maximum at 400 g casein/d. Milk yields and composition when glucose was infused resembled those seen on the zero casein treatment. 3. N-balance measurements indicated a severe deficit (-20 g/d) on the zero casein treatment and a progressive increase to +7 g/d as casein increased; N equilibrium was achieved at about 400 g casein/d. The regression of net productive N on N intake (P less than 0.001) indicated that the efficiency of utilization of dietary N did not differ between treatments. 4. Heat production increased with increase in casein infused (P less than 0.05) but remained a constant proportion of the metabolizable energy (ME) intake. Energy balances were negative and did not differ significantly between treatments but calculation of the protein and fat components indicated a threefold increase in body fat mobilization in response to the first increment of casein. Milk yield adjusted to zero energy balance was significantly related to ME intake (P less than 0.001) but the efficiency of energy utilization was not affected by the level of casein infusion. 5. The concentrations of glucose, beta-hydroxybutyrate and non-esterified fatty acids in plasma did not differ between treatments but the concentration of urea in plasma increased markedly (P less than 0.05) at the highest level of casein addition. Insulin concentrations increased and growth hormone decreased (both P less than 0.05) with increase in casein infusion. 6. The concentration of total amino acids (AA) in plasma increased up to 400 g casein/d and then declined. Changes in concentration and in the ratio of essential:total AA indicated a very high extraction rate of essential AA at the lower levels of casein infusion. 7. The observed lactational responses are discussed in relation to the ratio of protein:energy in the absorbed nutrients.(ABSTRACT TRUNCATED AT 400 WORDS)

Abomasum↗
PubMed1997

Comparison of growth performance and nutrient retention of weaner pigs given diets based on casein, free amino acids or conventional proteins.

In two experiments the potential value of diets based on casein or free amino acids (FAA) for amino acid utilization experiments were examined. In Expt 1 the optimum dietary electrolyte balance (dEB) for a casein-based diet was estimated by supplemention with 10 or 20 g NaHCO3/kg, to produce diets containing 64, 183 or 302 mmol/kg. In addition, piglet growth performance and efficiency of nutrient deposition of piglets given the casein diets were compared with two multiple protein source diets; Supercreep, a commercial multiple protein source diet or CFS (casein-fish-soyabean-sugar) or a FAA-based diet. Expt 2 was designed to compare piglet response to FAA diet stored at -15 degrees with twice daily feeding, with FAA diet stored at ambient temperature (13-30 degrees) and offered ad libitum. A CFS diet was used as a positive control and the experiment was conducted over the 10-20 kg growth phase. Expt 1 used forty-eight piglets weaned at 20-22 d of age and allocated to one of six treatments formulated to contain at least 0.84 g lysine/MJ digestible energy in a randomized block design. Piglets given the CFS and Supercreep diets produced superior growth rates (518, 491 g/d) to those given a FAA diet (353 g/d) or casein diet containing 0, 10 or 20 g NaHCO3/kg respectively (365, 417, 390 g/d) between 5 and 20 kg live weight. Piglets given the casein and FAA diets had higher amino acid digestibilities than those given the Supercreep and CFS diets. The increase in the dEB of the casein diet from 64 to 183 mmol/kg improved piglet growth performance between 5 and 20 kg by 14%. All piglets given casein diets had similar ileal and faecal digestibilities, empty-body compositions, nutrient deposition rates and retention ratios. The results of Expt 2 showed that there was no beneficial effect on piglet performance of storing the FAA diet at -15 degrees and feeding twice daily. Based on the results of these two experiments, neither the casein (0, 10, 20 g NaHCO3/kg) nor FAA diets were suitable for estimating amino acid utilization by the piglet. There remain unidentified factors which limit the growth performance of piglets given the casein and FAA diets.

Amino Acids↗
PubMed1980

Serum and liver lipids in growing rats fed casein with L-lysine.

Liver and serum lipid conentrations were studied in rats fed 7.5, 15 and 30% casein supplemented with 0, 2.5 and 5% lysine. Increasing dietary casein from 7.5 to 15% increased serum total lipids, triglycerides and cholesterol. When casein was increased from 15 to 30%, there was a further increase in plasma cholesterol and a decrease in triglycerides. Rats fed 7.5% casein alone developed fatty livers. Adding 5% lysine to 15% casein caused fatty livers but prevented them with casein at 7.5%. Lysine had no effect on total liver lipids with casein at 30%. The lipids of the fatty livers with 7.5% casein or with lysine were similar in composition. In both cases liver triglycerides increased fourfold and cholesterol twofold. Phospholipids remained unchanged and liver glycogen decreased. Excess dietary lysine did not change serum lipids ang glucose significantly. The data show that excess lysine caused changes in lipid metabolism which varied with the quantity of casein fed. The hypercholesterolemia with casein feeding seen by others appears unrelated to the high lysine content of this protein.

Animals↗
PubMed1999

Concentrations and anti-Haemophilus influenzae activities of beta-casein phosphoforms in human milk.

BACKGROUND: The distribution and concentrations of six phosphorylated forms of human beta-casein, a major source of nutrition among breast-fed infants, have not been examined in milk samples without prior fractionation. In this study, the levels of beta-casein phosphoforms in untreated human milk samples were analyzed and their antiadhesion activities determined against Haemophilus influenzae, a pathogen implicated in middle ear infection in infants. METHODS: Human milk samples were analyzed using urea-polyacrylamide gel electrophoresis of whole-milk samples and scanning densitometry to determine the concentrations of beta-casein and its phosphoforms. A nontypable H. influenzae strain was radiolabeled to monitor its attachment to human pharyngeal cells in microtiter plates. Purified phosphoforms of beta-casein were preincubated for 15 minutes with radiolabeled bacteria to determine their antiadhesion activities. RESULTS: The average beta-casein concentration in 151 human milk samples was 5.37+/-2.26 mg/ml. On average, the phosphoforms in untreated milk are present in the following order ranked by concentration: tetra- > di- > non- > mono- > tri- > pentaphosphorylated beta-casein. The tri-, tetra-, and pentaphosphorylated forms of human beta-casein exhibited more than 60% inhibition of H. influenzae in the antiadhesion assay when used at a concentration of 0.6 to 0.9 mg/ml. CONCLUSION: The beta-casein level in untreated human milk is significantly higher than previously reported. The phosphoform distribution of beta-casein in individual donors varies widely. Anti-H. influenzae activity was detected in vitro among human beta-casein molecules with three or more phosphate groups.

Antiviral Agents↗