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PubMed1990

Unequal distribution of a stable isotopic calcium tracer between casein and whey fractions of infant formulas, human milk and cow's milk.

Measurement of calcium absorption with tracers assumes a complete equilibration of tracer with milk calcium. In this study, the equilibration of tracer between the micellar casein and soluble fractions (primarily whey) of infant formulas, human milk and cow's milk was measured in vitro using milk samples enriched with 42Ca and analyzed by thermal ionization mass spectrometry. Incomplete equilibration of tracer occurred with the micellar casein fraction of all milks. The least equilibration with micellar casein was found with premature infant formula, for which the ratio of slopes of the equilibration lines (whey/casein) was 8.5/1. These differences may be due to Ca-casein binding in cow's milk-based formulas. The effects of the lack of tracer equilibration in vivo cannot be determined. However, unequal bioavailability of casein- vs. whey-bound Ca may exist.

Absorption↗
PubMed1991

Inhibitory effect of dietary soybean protein vs. casein on magnesium absorption in rats.

The effects of casein and soybean protein on magnesium absorption and magnesium concentration in the femur were investigated in rats. Purified diets containing either casein or soybean protein and three concentrations of added magnesium (0.82, 1.64 or 2.46 mmol/100 g diet) were used. The isonitrogenous diets were carefully balanced for the different mineral concentrations in the protein preparations. Absolute and percent magnesium absorption and urinary magnesium excretion were significantly decreased in rats fed soybean protein when compared with casein, irrespective of the dietary concentration of added magnesium. The magnesium content of femur was significantly lower in rats fed soybean protein, but this effect was seen only when the diet contained 0.82 mmol magnesium/100 g diet. The addition of sodium phytate to the casein diets, to a concentration identical to that in the diets containing soybean protein as provided by the soybean protein preparation, produced similar effects on magnesium absorption as the diets containing soybean protein. These results indicate that soybean protein, when compared with casein, decreases magnesium absorption through its phytate component.

Animals↗
PubMed1992

Bone composition and histology of young growing rats fed diets of varied calcium bioavailability: spinach, nonfat dry milk, or calcium carbonate added to casein.

Bone composition and histology were evaluated in young growing rats fed nutritionally complete but calcium-restricted (0.15%) diets in which calcium was derived from spinach, nonfat dry milk (NFDM), or CaCO3 added to casein. Groups of male weanling rats were pair-fed for 28 d. A 0.5% calcium casein-based diet group fed ad libitum was included to provide a comparison of normal bone structure and composition. Bone growth and bone ash were depressed in spinach-fed rats. Total bone tibia calcium in 0.5% calcium casein-based, 0.15% calcium casein-based, NFDM and spinach diet groups were 64.0, 29.2, 30.7 and 13.8 mg, respectively. All other measured bone mineral levels were also lower, except for potassium. Femur hydroxyproline concentrations were 1.2, 1.6, 1.6 and 2.1% in 0.5% calcium casein-based, 0.15% calcium caseinbased, NFDM and spinach diet groups, respectively. Bone histomorphometry indicated gross underdevelopment and compromised mineralization of trabecular bone of spinach-fed rats. For the first time, it has been demonstrated with histologic techniques that calcium from the low bioavailable source, spinach, compromises both the quantity and quality of bone. In contrast, when calcium is fed to growing animals at levels below the National Research Council requirement but from a highly bioavailable source (i.e., NFDM and CaCO3), there is only a reduction in bone quantity.

Animals↗
PubMed2005

Casein and soy protein meals differentially affect whole-body and splanchnic protein metabolism in healthy humans.

Dietary protein quality is considered to be dependent on the degree and velocity with which protein is digested, absorbed as amino acids, and retained in the gut as newly synthesized protein. Metabolic animal studies suggest that the quality of soy protein is inferior to that of casein protein, but confirmatory studies in humans are lacking. The study objective was to assess the quality of casein and soy protein by comparing their metabolic effects in healthy human subjects. Whole-body protein kinetics, splanchnic leucine extraction, and urea production rates were measured in the postabsorptive state and during 8-h enteral intakes of isonitrogenous [0.42 g protein/(kg body weight . 8 h)] protein-based test meals, which contained either casein (CAPM; n = 12) or soy protein (SOPM; n = 10) in 2 separate groups. Stable isotope techniques were used to study metabolic effects. With enteral food intake, protein metabolism changed from net protein breakdown to net protein synthesis. Net protein synthesis was greater in the CAPM group than in the SOPM group [52 +/- 14 and 17 +/- 14 nmol/(kg fat-free mass (FFM) . min), respectively; P < 0.02]. Urea synthesis rates decreased during consumption of both enteral meals, but the decrease tended to be greater in the subjects that consumed CAPM (P = 0.07). Absolute splanchnic extraction of leucine was higher in the subjects that consumed CAPM [306 +/- 31 nmol/(kg FFM . min)] vs. those that consumed SOPM [235 +/- 29 nmol/(kg FFM . min); P < 0.01]. In conclusion, a significantly larger portion of soy protein is degraded to urea, whereas casein protein likely contributes to splanchnic utilization (probably protein synthesis) to a greater extent. The biological value of soy protein must be considered inferior to that of casein protein in humans.

Adult↗
PubMed1992

Purification and characterization of two casein kinases from ejaculated bovine spermatozoa.

Two protein kinases active on casein and phosvitin were partially purified from the soluble fraction of ejaculated bovine spermatozoa. They were operationally termed casein kinase A and B based on the order of their elution from a phosphocellulose column. CK-A showed an approximate molecular mass of 38 kDa, and it phosphorylated serine residues of casein and phosvitin utilizing ATP as a phosphate donor (Km 19 microM). Enzyme activity was maximal in the presence of 10 mM MgCl2, whereas it decreased in the presence of spermine, polylysine, quercetin, and NaCl (20-250 mM). CK-B seemed to have a monomeric structure of about 41 kDa; it underwent autophosphorylation and cross-reacted with polyclonal antibodies raised against recombinant alpha, but not beta, subunit of human type 2 casein kinase. It phosphorylated both serine and threonine residues of casein and phosvitin, utilizing ATP (Km 12 microM) but not GTP as a phosphate donor. Threonine was more affected in the phosphorylated phosvitin than in the partially dephosphorylated substrate. CK-B was active toward the synthetic peptide Ser-(Glu)5 and calmodulin (in the latter case, in the presence of polylysine), and it was activated by spermine, polylysine, MgCl2 (30 mM), and NaCl (20-400 mM). The activity of the enzymes was not affected by cAMP, or the heat-stable inhibitor of the cAMP-dependent protein kinase, or calcium.

Animals↗
PubMed1982

A simple and sensitive proteinase assay using Sepharose 4B-coupled fluorescamine-labeled casein as a substrate.

A simple and sensitive method for proteinase assay was developed, which uses fluorescamine-labeled casein-Sepharose 4B as a substrate. Casein-Sepharose 4B was prepared most effectively by coupling casein to cyanogen bromide-activated Sepharose 4B at pH 10.0. Fluorescamine-labeled casein-Sepharose 4B was then prepared by mixing fluorescamine and casein-Sepharose 4B suspension at pH 8.0 and used for the assay as a substrate after removal of the excess reagent and/or its hydrolysis products. The assay can be done by simple measuring the fluorescence (excitation at 390 nm and emission at 475 nm) of the filtrate of the assay mixture after incubation of the substrate with enzyme solution. This method is suited for the assay of proteinases active at neutral to slightly alkaline pH values, and the activity of 3 ng of trypsin or 10 ng of alpha-chymotrypsin can be determined with reasonable accuracy. This method is therefore almost as sensitive as those using radioisotope-labeled proteins as substrates.

Animals↗
PubMed1996

Evidence from milk casein genes that cetaceans are close relatives of hippopotamid artiodactyls.

The inferred transition from terrestrial hoofed mammal to fully aquatic cetacean has been intensively studied with fossil evidence. However, large sections of this remarkable evolutionary sequence are missing. Phylogenetic analysis of extant taxa may help to fill in some of these gaps. In this report, kappa-casein (exon 4) and beta-casein (exon 7) milk protein genes from cetaceans and other placental mammals were PCR-amplified, sequenced, and aligned to previously published sequences. Phylogenetic analyses of the casein data suggest that hippopotamid artiodactyls are more closely related to cetaceans than to other artiodactyls (even-toed hoofed mammals). An analysis of the nuclear casein sequences combined with published mitochondrial cytochrome b DNA sequences also supports the Cetacea/Hippopotamidae sister group. This affinity implies that some of the aquatic traits of cetaceans were derived in the common ancestor of Cetacea and Hippopotamidae. An extant "missing link" to Cetacea may have been overlooked by science since the description of the semiaquatic Hippopotamus in 1758. Paleontological information is grossly inconsistent with this hypothesis. If the casein phylogeny is accurate, large gaps in the fossil record as well as extensive morphological reversals and convergences must be acknowledged.

Amino Acid Sequence↗
PubMed2000

Zinc homeostasis in healthy infants fed a casein hydrolysate formula.

BACKGROUND: The results of earlier, nonquantitative studies suggested that absorption of zinc from a semielemental (casein hydrolysate) formula was inferior to absorption from a cow's milk-based formula. The objective of this study was to compare fractional, total and net zinc absorption, and fecal excretion of endogenous zinc in the same healthy young infants when fed a casein hydrolysate versus cow's milk-based formula. METHODS: Fractional absorption of zinc and fecal excretion of endogenous zinc were determined from measurement of cumulative fecal excretion of unabsorbed tracer and by an isotope dilution technique, respectively, after oral administration of a 70Zn tracer with all formula feedings for 1 day. Six infants were assigned randomly to receive the test or control formula, and the other formula was administered 2 to 5 weeks later. RESULTS: Mean (+/-SD) fractional absorption of zinc from the casein hydrolysate formula (0.47 +/- 0.17) was double that from the cow's milk-based formula (0.22 +/- 0.04; P = 0.01) with a correspondingly greater total zinc absorption (3.23 +/- 1.67 mg Zn/day vs. 1.55 +/- 0.55 mg Zn/day; P = 0.05). Because the excretion of endogenous zinc in the feces did not differ between formulas (0.90 +/- 0.44 mg Zn/day vs. 0.91 +/- 0.29 mg Zn/day), net absorption of zinc was also higher with the casein hydrolysate formula (2.33 +/- 1.65 mg Zn/day vs. 0.81 +/- 0.67 mg Zn/day; P = 0.02). CONCLUSIONS: Retention of zinc appeared to be adequate to meet the needs for growth during feeding with cow's milk-based formula and was more than adequate during short-term feeding with the casein hydrolysate formula.

Absorption↗
PubMed1992

DNA binding activity of the Arabidopsis G-box binding factor GBF1 is stimulated by phosphorylation by casein kinase II from broccoli.

To study the phosphorylation of one of the G-box binding factors from Arabidopsis (GBF1), we have obtained large amounts of this protein by expression in Escherichia coli. Bacterial GBF1 was shown to be phosphorylated very efficiently by nuclear extracts from broccoli. The phosphorylation activity was partially purified by chromatography on heparin-Sepharose and DEAE-cellulose and was characterized. It showed the essential features of casein kinase II activity: utilization of GTP in addition to ATP as a phosphate donor, strong inhibition by heparin, preference for acidic protein substrates, salt-induced binding to phosphocellulose, and salt-dependent deaggregation. The very low Km value for GBF1 (220 nM compared to approximately 10 microM for casein) was in the range observed for identified physiological substrates of casein kinase II. Phosphorylation of GBF1 resulted in stimulation of the G-box binding activity and formation of a slower migrating protein-DNA complex. The conditions of this stimulatory reaction fully corresponded to the properties of casein kinase II, in particular its dependence on the known phosphate donors. The DNA binding activity of the endogenous plant GBF was shown to be reduced by treatment with calf alkaline phosphatase; this reduction was diminished by addition of fluoride and phosphate or incubation in the presence of casein kinase II and ATP.

Brassica↗
PubMed1991

Analysis of polymorphism in the bovine casein genes by use of the polymerase chain reaction.

Methods have been devised for detecting polymorphisms in the bovine beta- and kappa-casein genes using the polymerase chain reaction (PCR) followed either by restriction enzyme digestion (to reveal a restriction fragment length polymorphism (RFLP] or by hybridization of an allele-specific oligonucleotide. These methods, as well as being faster and more sensitive than traditional RFLP methods, are of more general applicability since they can detect any change in DNA sequence. They require only a small sample of blood or semen and are applicable to animals of any age or sex. These methods make possible large-scale screening and thus selection for alleles at these loci. Typing of blood DNA can give erroneous results when the animal concerned is a twin; however, this can be overcome by retesting using milk or semen. Analysis of the kappa-casein genotype of Holstein-Friesian bulls gives frequencies for the A and B alleles of 0.80 and 0.20 respectively. Selection in favour of the B allele, which is superior for cheese production, could thus have a large effect. The A3 and B alleles at the beta-casein locus have been shown to be rare in the Holstein-Friesian population. Linkage disequilibrium exists between beta-casein B and kappa-casein B.

Alleles↗
PubMed1992

Detection of bovine alpha s1-casein genomic variants using the allele-specific polymerase chain reaction.

A method was developed to distinguish between genotypic variants B and C of bovine alpha s1-casein, using the allele-specific polymerase chain reaction (ASPCR). The alpha s1-casein genotype determined for 17 Jersey cows by the ASPCR method was confirmed by typing the alpha s1-casein milk proteins on isoelectric focusing gels. Using the ASPCR method described, rapid analysis of the alpha s1-casein genotype of bulls is now possible. In addition, kappa-casein genotypes can be determined from the same PCR reaction.

Alleles↗
PubMed1994

RFLP and linkage analysis of the porcine casein loci--CASAS1, CASAS2, CASB and CASK.

Restriction fragment length polymorphisms (RFLPs) were revealed at the porcine casein loci with the following combinations of restriction endonucleases and porcine cDNA clones: alpha s1-casein (TaqI); alpha s2-casein (BamHI); and beta-casein (SacI). These RFLPs were shown to be under simple monogenic control by segregation analysis of two- and three-generation families. The CASAS1, CASAS2 and CASB casein loci were also shown to be linked with no recombinant haplotypes observed amongst 77 meioses in Large White and Meishan F1 and F2 crosses. No recombinants were observed in a further 106 meioses that were informative for linkage between CASAS1 and CASAS2.

Alleles↗
PubMed1996

Allergenic epitopes of bovine alpha S1-casein recognized by human IgE and IgG.

B-cell epitopes of bovine alpha S1-casein, one of the major allergens of cow's milk, were identified by a screening method based on synthetic peptides. According to the known amino acid sequence of alpha S1-casein, a set of 188 overlapping sequential decapeptides shifted by one amino acid was manually synthesized on polyethylene pins by the 9-fluorenyl-methoxycarbonyl (Fmoc) method. Peptides were screened by an enzyme-linked immunosorbent assay (ELISA) specific for human IgE and IgG. Bound antibodies were detected by successive incubation with up to three polyclonal antibodies, the last one conjugated to horseradish peroxidase. Tested sera were from 15 patients with acute clinical reactions to cow's milk and IgE-specific reactions to bovine alpha-casein in the ELISA and immunoblot. Sera from 10 healthy subjects without remarkable reactions to cow's milk proteins were used as controls. All sera from allergic subjects showed reactions with three regions of alpha S1-casein, corresponding to amino acids 19-30, 93-98, and 141-150. Furthermore, individual sera showed reactions with other parts of the protein. No essential differences in the epitope specificity of IgE and IgG were found. Inhibition of IgE binding to alpha S1-casein with soluble synthetic peptides confirmed the results and revealed peptide CN-2 as the most inhibiting one.

Adolescent↗
PubMed1994

Study of tensioactive properties of casein signal peptides and their interactions with phospholipids.

The high degree of sequence conservation in casein signal peptides reflects their unique functional properties. A series of casein signal peptides and derivatives was synthesized in order to study their insertion in phospholipidic mono- and bilayer structures. Most of these amphiphilic peptides were found to be highly tensio-active. Their conformations differ and are solvent dependent. Fluorescence anisotropy measurements showed that all the peptides of the series could interact with dimyristoylphosphatidyl -choline and -glycerol when mixed with the lipids prior to hydration of the liposomes. The most soluble peptide, P6, was selected for insertion experiments in multilamellar vesicles. Its interaction with liposomes is efficient and rapid, being temperature dependent. On the one hand, the physico-chemical measures of interactions of signal peptides of casein beta and alpha s2 confirm their mutual genetic relationship, and on the other hand they show the divergence of casein beta and alpha s2 from casein kappa signal peptide.

Amino Acid Sequence↗
PubMed1981

Substrate specificity of the nuclear protein kinase NII from porcine liver. Studies with casein variants.

The substrate specificity of the nuclear protein kinase NII from pig liver was studied using purified casein variants alpha s1B and beta A2 both in the phosphorylated and dephosphorylated form. Chymotryptic peptides of the phosphorylated casein were analyzed by ascending thin-layer chromatography followed by thin-layer electrophoresis. Phosphorylated peptides were detected by autoradiography. The determination of a phosphorylated site in a cluster of three serinees was performed by solid phase Edman degradation of the whole beta A2 casein. Phosphorylated beta A2 casein was by far the best substrate. A threonine at position 41 in the amino acid sequence was found to be predominantly phosphorylated. Dephosphorylated beta A2 casein became rephosphorylated at serine-17 whereas phosphorylated at threonine-41 was greatly reduced. In both sites acidic amino acid side chains are present at the C-terminal side though at different positions suggesting that acidic residues in the vicinity of the serin or threonine residue to be phosphorylated play an important role in the recognition by the nuclear protein kinase NII.

Amino Acid Sequence↗
PubMed1983

The insulin-stimulated receptor kinase is a tyrosine-specific casein kinase.

Insulin stimulates a kinase that phosphorylates tyrosines in the insulin receptor; this kinase is tightly associated with the insulin receptor itself. We now show that the insulin-stimulated casein kinase, present in solubilized, lectin-purified receptor preparations from rat liver, is indistinguishable from the insulin receptor kinase. As with phosphorylation of the insulin receptor, insulin selectively enhanced by 2-3-fold the phosphorylation of tyrosines in casein. The insulin-stimulated activities of both kinases were inactivated at 37 degrees C with the same t0.5 of 5 min and were identically affected by alkylating agents. Both receptor and casein kinase activities were specifically coprecipitated by anti-receptor antibodies or by insulin and anti-insulin antibodies. When the latter type of immune complexes were incubated with an excess of insulin, both kinase activities were quantitatively recovered. We therefore conclude that insulin-stimulated receptor and casein phosphorylations are probably catalyzed by a single enzyme which is tightly associated with the receptor itself. Now, by replacing casein for receptor as substrate, it is possible to measure the enzymatic activity of this receptor-related kinase itself, i.e. independent of the receptor as substrate. Detection of this activity is improved in the presence of certain alkylating agents. Use of artificial substrates (in combination with alkylating agents) is particularly important to dissect the functional components of the receptor complex, to study mechanisms of enzyme regulation and especially in situations where the available receptor for study is limited, e.g. fresh or cultured cells from patients.

Amino Acids↗
PubMed1984

Detection of type-2 casein kinase and its endogenous substrates in the components of the microsomal fraction of rat liver.

Rat liver type-2 casein kinase-TS (Ck-TS) is unevenly distributed among the different components of the rat liver post-mitochondrial particulate fraction: while it accounts for the whole casein kinase activity of protein-glycogen particles, it is absent in the microsomal membranes (exhibiting exclusively casein kinase activity of type-1) and coexists with type-1 casein kinase in ribosomes. At least seven proteins whose phosphorylation is promoted by Ck-TS have been detected in these fractions. The only important target of Ck-TS in protein-glycogen particles is a rather heterogeneous protein of Mr around 85000 which has been identified as glycogen synthase. Two polypeptides of Mr about 16000, possibly identifiable with acidic proteins P1 and P2, and an unidentified protein of Mr about 35000 are the main ribosomal substrates of Ck-TS. Three protein bands of Mr 52000, 79000 and 91000 are also very efficiently phosphorylated whenever the microsomal membranes, devoid of intrinsic casein kinase-2, are incubated with cytosolic Ck-TS. These membrane-bound radiolabeled proteins require deoxycholate for their solubilization: they are very acidic, according to their high affinity for DEAE-cellulose, and give rise to partially superimposable [32P]peptide maps, suggesting extensive homologies among them. They also exhibit a low affinity Ca2+ binding activity comparable to that of calsequestrin.

Animals↗
PubMed1985

Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland.

A serine-specific casein kinase, an integral membrane protein of the lactating guinea-pig mammary gland, has been purified from a Golgi-enriched membrane fraction, using a combination of sucrose gradient centrifugation and chromatography on ATP-agarose. The enzyme comprises a polypeptide of estimated Mr 74 000 as judged by sodium dodecyl sulphate/polyacrylamide gel electrophoresis, compared with a monomer Mr of 50 000 as determined by sucrose gradient centrifugation in the presence of 500 mM NaCl and 0.1% Triton X-100. Kinetic studies show that the purified enzyme exhibits kinetic constants distinctly different from the rabbit reticulocyte casein kinases I and II, whilst polyclonal antisera raised against the mammary gland enzyme did not cross-react with soluble liver or reticulocyte protein kinase activities. Immunoblotting and immunocytochemical analyses demonstrate the mammary gland enzyme's apparently unique location in lactating mammary gland tissue. Comparative studies with polyclonal antisera raised against bovine galactosyltransferase, show that casein kinase and galactosyltransferase have a similar intracellular localisation in the lactating mammary gland as judged by immunocytochemistry at the light level, but that casein kinase was unique to mammary gland whereas galactosyltransferase could be found in other tissues. The results extended our earlier observations which suggest a Golgi location for casein kinase, and demonstrate that future studies using this enzyme may well prove advantageous for the study of intracellular mechanisms involved in the biogenesis of organelles, in this instance the Golgi apparatus.

Animals↗