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PubMed1996

Allele frequencies of the major milk proteins in the Finnish Ayrshire and detection of a new kappa-casein variant.

A total of 20990 Finnish Ayrshire cows were phenotyped for the major milk proteins by isoelectric focusing in polyacrylamide gels. The predominant alleles in the Finnish Ayrshire were alpha S1-casein B (0.999), alpha S2-casein A (0.991), beta-casein A1 (0.509) and alpha 2 (0.490), kappa-casein A (0.612) and beta-lactoglobulin B (0.716). The kappa-casein E allele (0.307) was also rather common in the Finnish Ayrshire. A new kappa-casein variant (kappa-casein F) was demonstrated in two Finnish Ayrshire cows, a dam and a daughter.

Alleles↗
PubMed2006

Characterization of T cell epitopes in alphas1-casein in cow's milk allergic, atopic and non-atopic children.

BACKGROUND: One to two percent of infants suffer from IgE-mediated allergic reactions against cow's milk proteins. Most children develop clinical tolerance, but approximately 15% are still allergic by the age of 10 years. Little is known about the T cell epitopes in individual cow's milk protein in relation to allergy and tolerance. OBJECTIVE: To identify T cell epitopes in alphas1-casein, the most abundant milk protein, and to investigate T cell responses toward these epitopes in allergic, atopic and non-atopic children. METHODS: Allergen-specific T cell lines (TCLs) were derived from peripheral blood mononuclear cells of 11 cow's milk allergic, nine atopic and nine non-atopic children. T cell responses were measured to alphas1-casein and to overlapping peptides (18-mers), spanning the alphas1-casein molecule. Proliferation was determined by incorporation of (3)H-thymidine, and cytokine production (IL-10, IL-13 and IFN-gamma) was measured by ELISA. RESULTS: Four main regions (amino acid (AA) residues 43-66, 73-96, 91-114 and 127-180) in the alphas1-casein molecule were immunogenic to T cells, among which the AA residues 133-156 spanned the immunodominant part. Only subtle differences were found in peptide recognition between the subject groups. Some of the peptides induced slightly Th1- or Th2-skewed cytokine responses. The increased levels of IL-10 in response to alphas1-casein observed in TCLs from atopic children appeared not to be linked to recognition of specific IL-10-inducing epitopes. CONCLUSIONS: The immunodominant sequence in alphas1-casein is spanned by AA residues 133-156. Tolerance towards alphas1-casein in atopic children may be mediated by an overall induction of IL-10 and not by recognition of certain T cell epitopes. The identified T cell epitopes in children with cow's milk allergy may be useful targets in developing peptide immunotherapy.

Adolescent↗
PubMed1997

Allergenicity of alpha-caseins from cow, sheep, and goat.

The allergic potential of alpha-caseins from bovine, ovine, and goat's milk sharing more than 85% identical amino acids was compared. Caseins were purified by anion-exchange chromatography and used for a specific IgE and IgG ELISA with diluted human sera. Sera were from 17 children with immediate-type allergy to cow's milk, from 59 children with atopy but without food allergy, and from 27 healthy children without atopy disease. The sera of cow's milk-allergic children showed a significantly higher IgE and IgG binding to alpha-caseins from all three species than the sera of the other groups. All groups showed an increased antibody binding to bovine alpha-casein compared to the sheep and goat proteins, but the differences were significant only in the groups of atopic children and of healthy controls. Furthermore, inhibition of the IgE binding to bovine alpha-casein with alpha-casein from cow, goat, and sheep revealed that the alpha-casein from these species are highly cross-reactive; on the basis of the small differences in their primary structure. In conclusion, the milk of goat and sheep harbor an allergic potential and is not suitable for the nutrition of milk-allergic patients.

Animals↗
PubMed1986

Hormonally induced elevations of alpha- and beta-casein mRNA levels are blocked by cyclic adenine nucleotide and prostaglandins.

Normal mammary gland development during pregnancy follows a coordinated program of morphological development (formation of lobuloalveoli) and biochemical differentiation (casein production). In culture, whole mammary glands of Balb/c mice can be similarly induced by application of a mixture of insulin, prolactin, aldosterone and hydrocortisone (IPAH) for 7 days. Our previous reports have shown that lobuloalveolar development, induced by IPAH, is competitively inhibited by the simultaneous presence of dibutyryl cyclic AMP (Bt2cAMP), prostaglandins (PGs) E1, E2, and B1, and papaverine (pap). However, if this mixture is not added until day 4, lobuloalveolar development is relatively unaffected but casein synthesis is repressed. This report explores the mechanism by which cyclic adenine nucleotides and prostaglandins interfere with the normal developmental pathway. The accumulation of alpha- and beta-casein mRNAs induced by prolactin, hydrocortisone and aldosterone is blocked by the combination of Bt2cAMP, PGs E1, E2, and B1, and pap added to the medium for the final 3 days (days 4-7). Under these conditions the glands retain their lobuloalveoli, and little squamous metaplasia can be discerned. Furthermore, de novo synthesis of both caseins is selectively inhibited, despite the continued presence of casein mRNAs in the glands and normal protein synthesis. In contrast, the synthesis of keratin is stimulated. Incomplete mixtures of Bt2cAMP and pap or the combination of PGs E1, E2, and B1, are only partly effective in preventing the accumulation of casein mRNAs. All three mixtures bring about similar effects on both alpha- and beta-casein mRNAs.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1985

Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Identification of the sites phosphorylated by casein kinase-I.

A casein kinase was highly purified from rabbit skeletal muscle whose substrate specificity and enzymatic properties were virtually identical to those of casein kinase-I from rabbit reticulocytes. Prolonged incubation of glycogen synthase with high concentrations of skeletal muscle casein kinase-I and Mg-ATP resulted in the incorporation of greater than 6 mol phosphate/mol subunit and decreased the activity ratio (+/- glucose-6P) from 0.8 to less than 0.02. The sites phosphorylated by casein kinase-I were all located in the N and C-terminal cyanogen bromide peptides, termed CB-1 and CB-2. At an incorporation of 6 mol phosphate/mol subunit, approximately equal to 2 mol/mol was present in CB-1 and approximately equal to 4 mol/mol in CB-2. Within CB-1, casein kinase-I phosphorylated the serines that were 3, 7 and 10 residues from the N-terminus of glycogen synthase, with minor phosphorylation at threonine-5. Within CB-2, approximately equal to 90% of the phosphate incorporated was located between residues 28 and 53, and at least five of the seven serine residues in this region were phosphorylated. The remaining 10% of phosphate incorporated into CB-2 was located between residues 98 and 123, mainly at a serine residue(s). Two of the major sites labelled by casein kinase-I (serine-3 and serine-10 of CB-1) are not phosphorylated by any other protein kinase. This will enable the role of casein kinase-I as a glycogen synthase kinase in vivo to be evaluated.

Amino Acid Sequence↗
PubMed1977

Kinetics of serum amyloid protein A in casein-induced murine amyloidosis.

Serum amyloid protein A (SAA), the precursor of secondary amyloid protein, is elevated in chronic diseases which are associated with an increased incidence of amyloid. However, SAA is also elevated in acute bacterial and viral infections and somes forms of cancer. The murine model of casein-induced amyloidosis was studied to determine the relationship between SAA production and amyloid deposition. SAA levels measured by radioimmunoassay were found to be as high as 200 times the normal level in CBA/J mice receiving daily parenteral casein. After a single injection of casein the SAA level was elevated by 3h and peaked by 12-18 h. Similar levels were found in casein-treated A/J mice, a strain less susceptible to the induction of amyloid. Parenterally administered bovine serum albumin, which has low potential for amyloid induction, gave SAA levels in CBA/J and A/J mice comparable to casein treatment. These data show that, while SAA levels are elevated during chronic antigenic stimulation, there are other factors involved in amyloid formation. These factors may include alterations in the degradation of SAA by the reticuloendothelial system caused by substances such as casein. Nude (athymic) mice were shown to attain high levels of SAA after receiving casein parenterally. Therefore, thymus-derived lymphocytes are not necessary for the synthesis of SAA.

Amyloid↗
PubMed1983

Interaction between bovine casein and V. cholerae enterotoxin in the rabbit ileal loop.

Secretory IgA from human breast milk neutralizes cholera enterotoxin in the rabbit ileal loop system. No similar protection by purified bovine milk proteins could be demonstrated; however, one bovine milk protein, casein, had a deleterious effect on intestine exposed to very small quantities of enterotoxin. Highly purified cholera toxin (10 or 100 ng) was incubated with bovine protein solutions for 60 min at 37 degrees C. One-milliliter aliquots were then injected into prepared rabbit intestine loops. The animals were sacrificed at 18 h and the intestinal loop contents were aspirated, and a volume to length of loop ratio (V/L) was determined. The activity of 100 ng of toxin was not enhanced by the majority of bovine milk proteins, but bovine casein caused a 14-40% increase in the fluid production (V/L of casein + toxin versus toxin, 1.05 versus 0.92 and 1.82 versus 1.30). All of the bovine proteins but casein inhibited the action of low dose enterotoxin. Bovine casein caused a 78-90% increase in fluid production by loops exposed to a suboptimal toxin dose (10 ng) (V/L of casein + toxin versus toxin, 1.12 versus 0.63 and 0.95 versus 0.50). Virtually all of this enhancement of enterotoxin fluid response resided in the purified alpha-casein fraction.

Animals↗
PubMed1994

Similar gastric emptying rates for casein- and whey-predominant formulas in preterm infants.

Casein-predominant infant milk formulas have been speculated to predispose to lactobezoar formation in preterm infants due to delayed gastric emptying. There have been, however, no prospective studies to prove this possibility. In a randomized, double-blinded, prospective study, we tested the hypothesis that preterm infants fed casein-predominant milk formula have slower gastric emptying than infants fed whey-predominant formulas. Twenty preterm infants within the first 4 d of life were randomized to receive either the whey-predominant formula Similac Special Care (whey:casein ratio 60:40) or an experimental casein-predominant formula (whey:casein ratio 18:82). Only the protein composition differed between the two formulas. The infants were fed the assigned study formula until they reached approximately 2200 g body weight when a gastric emptying scan was performed, using the designated study formula mixed with 25 microCi of technetium-99 sulfur colloid. Gastric emptying was followed continuously for 2 h. Gastric emptying at 30, 60, 90, and 120 min was similar between the two study groups. The time for 50% gastric emptying was 64.9 +/- 12.3 min for the infants fed the whey-predominant formula and 56.5 +/- 14.8 min for those fed the casein-predominant formula (p = 0.75). We conclude that the rate of gastric emptying in preterm infants fed casein-predominant formulas is similar to that in those fed whey-predominant formulas.

Animals↗
PubMed2004

The liver-enriched inhibitory protein isoform of CCAAT/enhancer-binding protein beta, but not nuclear factor-kappaB, mediates the transcriptional inhibition of beta-casein by tumor necrosis factor-alpha.

TNF-alpha is a physiological regulator of mammary gland development that stimulates the growth of both normal and malignant mammary epithelial cells in primary culture and inhibits functional differentiation. To understand how TNF exerts its effects, the current study examined the mechanism by which TNF down-regulates expression of the beta-casein and whey acidic protein (WAP) genes. TNF treatment markedly decreased activity of the beta-casein and WAP promoters in transiently transfected HC11 mammary epithelial cells. Overexpression of the nuclear factor-kappaB (NFkappaB) p50 and/or p65 proteins increased the transcriptional activity of the beta-casein and WAP promoters in HC11 cells, suggesting that the inhibitory effect of TNF on transcription of these genes is not mediated by NFkappaB. This was further confirmed in experiments in which an NFkappaB super-repressor was overexpressed, and by deletion of an NFkappaB binding site in the beta-casein promoter. In contrast, we found that TNF induced both nuclear expression and the DNA-binding activity of liver-enriched inhibitory protein (LIP) isoform of CCAAT/enhancer-binding protein beta. Moreover, cotransfection of LIP and beta-casein expression vectors showed that LIP suppressed the transcriptional activity of the beta-casein promoter. Together, these results suggest that LIP plays a critical role in mediating TNF-induced down-regulation of the beta-casein gene.

Animals↗
PubMed1989

Spermidine is necessary for, but not the only mediator of, linoleic acid-stimulated alpha-casein accumulation in mouse mammary epithelial cells.

Mammary epithelial cells obtained from virgin mice were induced to accumulate alpha-casein in serum-free two-stage collagen gel culture with insulin, PRL, and linoleic acid. Omission of either PRL or linoleic acid drastically reduces alpha-casein accumulation. Spermidine addition to insulin-containing medium in either the absence or presence of linoleic acid does not stimulate alpha-casein accumulation. We conclude from this that spermidine can not be the sole mediator of PRL action. Spermidine also will not replace linoleic acid for alpha-casein accumulation if the fatty acid is omitted from the culture medium and will not increase casein accumulation when supplemented into PRL- and linoleic acid-containing medium; thus, it is not the sole mediator of linoleic acid action. However, the spermidine synthesis inhibitor methylglyoxal-(bis)-guanylhydrazone does inhibit alpha-casein accumulation in a concentration-dependent and spermidine-recoverable manner in cells stimulated by PRL and linoleic acid. We could not detect changes in polyamine levels in response to any of the medium supplements used in this investigation. Spermidine is, thus, at least a required comediator of the alpha-casein synthesis induction, although its role remains enigmatic.

Animals↗
PubMed1992

Progesterone regulation of a pregnancy-specific transcription repressor to beta-casein gene promoter in mouse mammary gland.

Progesterone inhibits casein gene expression in the mammary gland during pregnancy. A pregnancy-specific mammary nuclear factor (PMF) is a transcriptional repressor that binds to the two separate sites of the beta-casein promoter region and mediates the inhibition of mouse beta-casein gene expression by progesterone. PMF has been detected in mouse mammary tissue during pregnancy, but not during the virginal or lactational periods. Southwestern hybridization showed that the PMF-binding sequence (TGAT/ATCA) bound a protein with a mol wt of 65 kilodaltons from mammary nuclear extract from pregnant mice, but not that from lactating animals. In this study the hormonal regulation of binding activity of PMF and its relationship to casein gene expression were also examined in vivo using ovariectomy of pregnant mice. Ovariectomy rapidly reduces the circulating progesterone and estrogen levels and induces lactogenesis in the mammary tissue of pregnant mice. After ovariectomy, the binding activity of PMF in the mammary gland was reduced to a very low level (< 5% of the sham-operated level) at 24 h, whereas the binding activity of another nuclear protein, octamer-like binding factor, was not altered 24 h after the operation. Progesterone injection at the time of ovariectomy inhibited the loss of PMF-binding activity, and the level of its activity was maintained at about 66% the level of sham-operated pregnant animals 24 h after steroid administration. The ability of progesterone to prevent the ovariectomy-mediated decrease in PMF-binding activity was specific, since other steroid hormones, such as estrogen, hydrocortisone, or testosterone, were incapable of doing so. In contrast to PMF, ovariectomy increased the level of beta-casein mRNA in mammary tissue, and this increase was inhibited by concomitant administration of progesterone, suggesting that the extent of beta-casein gene expression was inversely related to PMF-binding activity in mammary tissue. These results are consistent with the view that PMF plays a role in the regulation of casein gene expression by mediating the inhibitory action of progesterone.

Animals↗
PubMed1994

A combination of distal and proximal regions is required for efficient prolactin regulation of transfected rabbit alpha s1-casein chloramphenicol acetyltransferase constructs.

In the rabbit, alpha s1-casein is the major casein secreted in the milk. Transcription of the alpha s1-casein gene is induced by PRL. To define the positions of the cis-sequences involved in the control of rabbit alpha s1-casein gene expression by PRL, chimeric genes containing upstream regions of alpha s1-casein gene linked to the chloramphenicol acetyltransferase gene were cotransfected into Chinese hamster ovary cells with the plasmid expressing the rabbit mammary PRL receptor. It was observed that a distal fragment -3442/-3118 was responsible for a high induction of PRL sensitivity when linked in the 5'-position to a chimeric construct (-391/1774)-chloramphenicol acetyltransferase. A cooperation between distal and proximal regions of the alpha s1-casein gene is responsible for the PRL-dependent enhancer activity of the distal fragment. The mammary gland-specific nuclear factor-like binding sequence found around position -90 in the proximal promoter of the alpha s1-casein gene is involved in this cooperation. The distal fragment was further studied to determine the position of regulatory regions. A -3442/-3385 fragment was sufficient to induce a PRL sensitivity similar to that conferred by the larger -3442/-3118 distal fragment, but multiple interactions are likely to exist between other regulatory regions included in this distal fragment. Four DNA-binding regions (I-IV) have been identified within the reduced -3442/-3385 fragment by footprint experiments using rabbit mammary gland or liver nuclear extracts (NE). Protected area III is observed using both NE. Protected areas I, II, and IV are specific for lactating mammary gland NE. The sequences of areas I and IV share several homologies with the sequence of the mammary gland-specific nuclear factor-binding site.

Animals↗
PubMed1999

Guanidinated casein hydrolysate stimulation of cholecystokinin release via pancreatic enzyme- and cholinergic-independent mechanisms in rats.

We had demonstrated that a peptic hydrolysate of guanidinated casein that is made from casein by the conversion of lysine to homoarginine stimulated pancreatic exocrine secretion in rats with chronic bile-pancreatic juice (BPJ) diversion from the proximal small intestine. This modified protein also stimulated cholecystokinin (CCK) release from dispersed rat intestinal cells. In this study, we found that guanidinated casein hydrolysate stimulates CCK release in chronic BPJ-diverted rats with cholinergic control blocked by atropine. Intraduodenal guanidinated casein hydrolysate increased portal plasma CCK concentration and pancreatic secretion in atropine-treated BPJ-diverted rats. In contrast, the portal plasma CCK concentration was not increased by intact casein hydrolysate. We conclude that guanidinated casein hydrolysate directly stimulates CCK release from the intestine via some cholinergic-independent mechanism, and an increase of the pancreatic exocrine secretion is regulated by CCK released by guanidinated casein hydrolysate. A guanidyl residue is likely to be involved in this control.

Animals↗
PubMed2000

Different beta-casein fractions in Icelandic versus Scandinavian cow's milk may influence diabetogenicity of cow's milk in infancy and explain low incidence of insulin-dependent diabetes mellitus in Iceland.

OBJECTIVES: To compare children with insulin-dependent diabetes mellitus (IDDM) with controls in Iceland regarding their consumption of cow's milk in infancy, and to investigate the beta-casein fractions in Scandinavian and Icelandic cow's milk. The A1 variant of beta-casein has been shown to be diabetogenic in animal studies, and suggestions have been made that the B variant of beta-casein acts similarly. Differences in the relative proportions of beta-casein fractions might explain the lower incidence of IDDM in Iceland than in Scandinavia. METHODS: A retrospective case-control study on IDDM patients and matching controls was performed in Iceland to compare their diets in infancy. Fifty-five children with IDDM born in Iceland over a 16-year period and randomly collected controls (n = 165) were recruited to the study. Mothers of the children answered questions on breastfeeding habits and on when cow's milk products were introduced. Samples of cow's milk from randomly selected milk batches from the largest consumption areas in Iceland and Scandinavia were collected. The milk samples were freeze-dried and their beta-casein fractions were analyzed using capillary electrophoresis. RESULTS: No significant difference was found between IDDM patients and controls in the frequency and duration of breastfeeding or the first introduction of cow's milk products. The analyses of milk samples showed that the percentage of the A1 and B variants of beta-casein in Icelandic milk was significantly lower than in the milk from the Scandinavian countries. CONCLUSIONS: Cow's milk consumption in infancy is not related to IDDM in Iceland. The lower fraction of A1 and B beta-caseins in Icelandic cow's milk may explain why there is a lower incidence of IDDM in Iceland than in Scandinavia.

Adolescent↗
PubMed2006

Nutritional evaluation of caseins and whey proteins and their hydrolysates from Protamex.

Whey protein concentrate (WPC 80) and sodium caseinate were hydrolyzed by Protamex to 5%, 10%, 15%, and 20% degree of hydrolysis (DH). WPC 80, sodium caseinate and their hydrolysates were then analyzed, compared and evaluated for their nutritional qualities. Their chemical composition, protein solubility, amino acid composition, essential amino acid index (EAA index), biological value (BV), nutritional index (NI), chemical score, enzymic protein efficiency ratio (E-PER) and in vitro protein digestibility (IVPD) were determined. The results indicated that the enzymatic hydrolysis of WPC 80 and sodium caseinate by Protamex improved the solubility and IVPD of their hydrolysates. WPC 80, sodium caseinate and their hydrolysates were high-quality proteins and had a surplus of essential amino acids compared with the FAO/WHO/UNU (1985) reference standard. The nutritive value of WPC 80 and its hydrolysates was superior to that of sodium caseinate and its hydrolysates as indicated by some nutritional parameters such as the amino acid composition, chemical score, EAA index and predicted BV. However, the E-PER was lower for the WPC hydrolysates as compared to unhydrolyzed WPC 80 but sodium caseinate and its hydrolysates did not differ significantly. The nutritional qualities of WPC 80, sodium caseinate and their hydrolysates were good and make them appropriate for food formulations or as nutritional supplements.

Amino Acids↗
PubMed1992

Molecular characterization and in-vitro hormonal requirements for expression of two casein genes from a marsupial.

Two marsupial casein genes have been isolated from a tammar wallaby (Macropus eugenii) mammary gland cDNA library. Comparisons of the tammar alpha- and beta-casein genes with their eutherian homologous reveal extensive divergence at the levels of nucleotide and amino acid sequences. Regions of similarity between the tammar and eutherian Ca(2+)-sensitive caseins are restricted to the major phosphorylation sites and the signal peptides. Quantification of casein mRNA levels in hormone-stimulated mammary gland explants from tammars in late pregnancy suggests that maximal induction of the beta-casein gene is dependent upon prolactin and insulin, while maximal induction of the alpha-casein gene is dependent upon prolactin, insulin and cortisol. These results are in contrast to earlier studies which show that the maximal induction of a putative 19 kDa casein, alpha-lactalbumin and beta-lactoglobulin in the tammar mammary gland is dependent upon prolactin alone. The expression of the latter three genes is not modulated by other hormones known to play a role in the in-vitro initiation of lactation in eutherians.

Amino Acid Sequence↗
PubMed2000

Associations between casein haplotypes and milk production traits of Swiss Brown cattle.

Effects of casein haplotypes and beta-lactoglobulin (LG) genotypes on milk protein fractions and on daughter yield deviations for milk performance traits were estimated from a daughter design. Offspring of seven Swiss Brown sires with the haplotypes B-A-B-A and B-A-B-B for alpha s1-, alpha s2-, beta-, and kappa-caseins were selected. The milk of daughter groups with paternal haplotype B-A-B-A was associated with lower casein content and higher whey protein content compared with B-A-B-B. Because of these contrary effects, the true protein content was not affected by the paternal haplotypes. The effects of maternal haplotypes were significant on true protein and casein content but not on whey protein content. The beta-LG genotypes had highly significant effects on casein and whey protein content. The effect of beta-LG BB was positive on casein and negative on whey protein content compared with beta-LG AA; the effect of beta-LG AB was intermediate. No significant effects of paternal haplotypes were found for daughter yield deviation on kilograms of milk, fat, and protein or percentages of fat and protein. The effects of the beta-LG genotypes were, independent of the parental haplotypes, close to significant on daughter yield deviation for percentage of protein. The beta-LG BB tended to be associated with a higher protein content compared with beta-LG AA. The effects for beta-LG genotypes showed additive gene effects. The analysis of paternal haplotypes within sires revealed a contrary effect of haplotypes for two of the seven sires for casein content. The paternal haplotypes within sire showed, although not significant, that haplotypes of the two sires had a contrary effect on daughter yield deviation for percentage of protein as well.

Animals↗
PubMed2000

Addition of casein or whey protein to colostrum or a colostrum supplement product on absorption of IgG in neonatal calves.

The effects of the addition of nonimmunoglobulin protein on absorption of immunoglobulin G (IgG) from colostrum or colostrum supplement products were determined in two experiments. In experiment 1, 48 Holstein calves were fed 4 L of pooled maternal colostrum or 4 L of reconstituted colostrum supplement with 0, 200, or 400 g of added whey protein concentrate or casein. In experiment 2, 38 Jersey calves were fed 2 L of pooled maternal colostrum with 100 or 200 g of whey protein concentrate or casein added immediately before feeding. Blood was collected at 24 h of age and plasma IgG concentration, total protein, hematocrit (experiment 1 only), and plasma urea N were determined. In experiment 1, blood samples were also collected at 4, 8, 12, 16, and 20 h to evaluate absorption of IgG and protein and urea N concentrations. The addition of 400 g of casein to colostrum supplement in experiment 1 reduced plasma IgG from 5.66 g/L (0 g of casein addition) to 3.88 g/L, increased plasma urea N at 24 h, and reduced the change in plasma total protein from 0 to 24 h. Hourly plasma IgG concentrations increased with the consumption of colostrum or supplements but increased more rapidly in calves fed whey protein concentrate and more slowly in calves fed casein. The addition of 200 g of casein or whey protein concentrate to colostrum supplements had no effect on plasma IgG concentration at 24 h of age. The addition of 100 or 200 g of casein or whey protein concentrate to maternal colostrum had no effect on plasma urea N, total protein, or plasma IgG in experiment 2. The addition of nonimmunoglobulin protein to colostrum supplements or maternal colostrum did not affect IgG absorption from the intestine of newborn calves unless the amount of total protein exceeded 500 g of protein.

Animals↗