Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “CASEIN”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,117 records · Page 62Linked to original sources
PubMed1977

Effect of bovine plasmin on alpha-S1-B and kappa-A caseins.

Both alpha-S1- and kappa-caseins were incubated at 37 C in the presence of bovine plasmin (.28 mg/ml) prepared from fresh blood plasma. The electrophoretic pattern of kappa-casein A was unchanged following 60-min incubation with plasmin. However, the electrophoretic band corresponding to alpha-S1-casein B gradually disappeared during the initial 30-min incubation with plasmin. Proteolysis was accompanied by the formation of one polypeptide band with electrophoretic mobility slightly slower than alpha-S1-casein B and several bands with faster electrophoretic mobilities. Two of the faster electrophoretic bands contained phosphorus. Estimates of molecular weights were 20,500, 12,300, and 10,300 daltons for three of these early degradation products of alpha-S1-casein B by plasmin.

Animals↗
PubMed1978

Isolation and partial characterization of rate casein proteins.

Casein was isolated from rat milk by high speed centrifugation. Polyacrylamide disc gel electrophoresis of the whole casein yielded three major protein zones designated C.1, C.2, and C.3 in order of their decreasing electrophoretic mobility in the alkaline system. Zone 3 subsequently contained two possibly related bands, C.3.1 and C.3.2. The presence of phosphate in all four zones was indicated by staining and conformed by phosphorus-32 labeling studies. A glycoprotein character was indicated by all zones. Separation of the constituents of rat casein by diethylaminoethyl-cellulose ion exchange chromatography yielded the same four major protein entities. Three milk-specific phosphoproteins unique to rat whey cluted from such columns in the same general region as the casein constituents but appear to be otherwise unrelated to the four major components of micellar casein. Gel electrophoresis in sodium dodecyl sulfate systems yielded apparent molecular weight estimates of approximately 24,000 for C.1, 38,000 for C.2, and 28,000 for c.3.1 and c.3.2.

Animals↗
PubMed1982

Casein synthesis by mouse polysomes and their messenger ribonucleic acid extracts.

Mammary epithelial cells from lactating mice were used to compare the in vitro casein synthesis by membrane-bound and free polysomes with that of messenger ribonucleic acid extracted from free- and bound polysomes (polysomal system and a rabbit reticulocyte lysate system). Casein synthesis was detected by incorporation of hydrogen-3 labeled amino acids in the reaction mixture into synthesized casein molecules. Membrane-bound polysomes synthesized considerably more casein than free polysomes; this difference was abolished by deoxycholate treatment of free polysomes. The synthesizing activity of messenger ribonucleic acid was similar whether extracted from free- or membrane-bound polysomes. Casein synthesis may be controlled by factors on the polysomal membrane.

Animals↗
PubMed1987

Rapid method for determination of milk casein content by infrared analysis.

Preliminary work was to develop a method for determination of milk casein content using commercially available infrared milk testing equipment. Fresh whole milk samples were split into two portions. One portion was tested for total protein with an infrared milk analyzer. The other portion was adjusted to pH 4.6 with a specific volume and concentration of phosphoric acid. Milk casein precipitated at pH 4.6 and was removed by filtration. Next, the noncasein protein filtrate was tested for protein content using an infrared milk analyzer. The difference between the percent protein of the original milk sample and the percent protein of the noncasein protein filtrate equals the percent milk casein. The infrared casein determination for 36 different individual herd milk samples was not significantly different from results obtained by the official International Dairy Federation casein testing method. The infrared method is faster than the chemical method and could be done with infrared milk testing equipment that is commonly available in many cheese manufacturing plants. Repeatability of the infrared method was comparable to the repeatability of the chemical method.

Animals↗
PubMed1988

Casein gene expression in bovine mammary gland.

The objectives were to examine the rate of synthesis of casein mRNA transcripts in bovine mammary tissue at different hormonal states and to study the effects of hormonal stimuli (insulin, hydrocortisone, and prolactin) on the accumulation of casein mRNA and on the rate of protein secretion by epithelial cells from bovine mammary tissues. Total cytoplasmic RNA was extracted from mammary tissues of cows obtained by biopsy (8 mo pregnant) and upon slaughter (lactating). The relative specific activities of cytoplasmic mRNA for alpha s1-, alpha s2-, beta-, and kappa-casein were about 3.2, 4.6, 3.3, and 4.5-fold higher in tissues of lactating cows than in those of 8 mo pregnant cows. Mammary alveolar epithelial cells retained hormone-inducible milk protein gene expression for total milk protein gene expression for total milk protein secretion and for alpha s1- and beta-casein messages. Prolactin, even in the absence of insulin and hydrocortisone, induced significant amounts of milk protein mRNA. Hydrocortisone in the presence of prolactin amplified the lactogenic effects on mammary epithelium. Maximal induction of beta-casein mRNA and protein secretion occurred when all three hormones were present.

Animals↗
PubMed1990

Isolation of monoclonal antibodies monospecific for bovine kappa-casein.

Bovine kappa-casein represents a major portion of the total protein present in milk and is required for formation of the caseinate micelles responsible for the transportation of both calcium and phosphorous. Two monoclonal antibodies directed against bovine kappa-casein have been isolated. Both monoclonal antibodies are highly specific for bovine kappa-casein. Western analysis of denatured kappa-casein suggests epitope specificity is, in part, conformationally dependent. Additional epitope mapping with chymosin and neuraminidase also suggest antibody binding is in the region of the amino acid sequence Pro-Thr-Thr at positions 92 to 94 and 134 to 136.

Amino Acid Sequence↗
PubMed1992

Benzaldehyde, citral, and d-limonene flavor perception in the presence of casein and whey proteins.

The effect of sodium caseinate and whey protein concentrate on benzaldehyde, d-limonene, and citral flavor intensity was determined by quantitative descriptive analysis deviation from reference using a 12-member trained panel. The concentrations for the benzaldehyde, d-limonene, and citral flavor intensity references were 17.8, 53.0, and 19.8 ppm, respectively. The concentration for both protein references was .25%. Flavored protein solutions were held for 17 h at 6 degrees C and contained benzaldehyde (17.8 ppm), d-limonene (53 ppm), or citral (19.8 ppm) and 2.5% sucrose with 0, .125, .25, or .5% protein. Benzaldehyde flavor intensity declined as the whey protein concentrate concentration increased from 0 to .5%. There was no significant difference in benzaldehyde flavor intensity with casein compared with the reference. The d-limonene flavor intensity declined as the protein concentration increased. Panelists found no significant drop in citral flavor intensity with casein or whey protein. Decreased benzaldehyde and d-limonene flavor intensity in the presence of whey protein concentrate or casein may be due to nonpolar interactions (casein), interaction with nonpolar binding sites, cysteine-aldehyde condensation, or Schiff base formation (whey protein concentrate).

Acyclic Monoterpenes↗
PubMed1994

Effect of graded levels of duodenal infusions of casein on mammary uptake in lactating cows. 1. Major nutrients.

Effects of duodenally infused casein on milk secretion were investigated by coupling measurements of mammary blood flow and arteriovenous differences. Four lactating cows were given a continuous duodenal infusion of 0, 177, 352, and 762 g of calcium caseinate/d according to a Latin square design. Diets, formulated to meet 90% of energy and protein recommendations, consisted of a ratio of corn silage:concentrate of 76:24 supplemented with dehydrated alfalfa. Yields of milk, protein, and fat increased linearly with casein infusions (by up to 2.6 kg/d, 126 g/d, and 133 g/d, respectively) as did milk protein content (by up to 2.2 g/kg). Mammary blood flow and insulin, prolactin, and growth hormone in plasma were not affected by added casein. Concentrations of arterial acetate, glucose, BHBA, and NEFA remained unchanged, but their uptake by the udder increased by 3, 18, 22, and 91%, respectively, between the control and high casein treatments. Plasma arterial concentrations and the mammary uptake of essential and nonessential AA increased linearly with casein infusions. Although arterial concentrations increased to a much greater degree for essential AA than for nonessential AA, the increased udder extraction was higher for nonessential AA. The main part of the added AA (90%) was extracted by the udder. However, a direct transfer of supplementary-extracted AA into milk did not occur, thus increasing AA availability for other metabolic pathways.

3-Hydroxybutyric Acid↗
PubMed1996

A method for isolating beta-casein.

A new method was developed for obtaining pure beta-CN. Calcium caseinate (3%) was reconstituted, renneted to form a gel, cooled (4 degrees C) to allow beta-CN dissociation from the caseinate gel, and centrifuged. The supernatant was warmed to 30 degrees C, precipitating pure beta-CN from solution. Large quantities of beta-CN were recovered by scaling-up this procedure, but these beta-CN preparations were less pure than the beta-CN that was prepared on a smaller scale. Chromatography (FPLC) and urea-PAGE showed beta-CN to be the main component in the precipitate. Chymosin, used to form the caseinate gel, did not extensively hydrolyze beta-CN under the conditions of these experiments. Calcium concentration, cooling time, and caseinate concentration influenced the recovery of beta-CN. Maximum recovery of beta-CN, under the experimental conditions used, occurred at 10 mM calcium, 48 h of cooling, and 3% caseinate concentration.

Calcium↗
PubMed1997

Marked effect of beta-lactoglobulin polymorphism on the ratio of casein to total protein in milk.

The relationship between genetic variants for milk protein and the composition of milk was analyzed on 4475 repeated milk samples from individual cows; 371 dairy cows of the Swedish Red and White breed and 204 cows of the Swedish Holstein breed were used. The registrations included percentages of casein, protein, fat, and lactose in combination with milk yield and SCC. The genotype of individual cows for alpha(s1)-CN, beta-CN, kappa-CN, and beta-LG was determined by alkaline and acidic PAGE. A mixed animal model was used for the analysis; beta-LG and aggregate casein genotypes were included simultaneously as separate fixed effects in the statistical model. The results suggest a positive additive effect of the beta-LG B allele on casein content and on the ratio of casein to total protein. For the latter trait, the beta-LG genotype accounted for a relatively large part of the phenotypic variance, corresponding to a reduction in residual variance of 11% when included in the model. The corresponding value for casein content was 0.5%. The lack of unfavorable associations between milk protein variants and the traits included in this study makes the beta-LG gene an obvious candidate when the breeding objective is improved conversion of milk protein into cheese.

Animals↗
PubMed1977

Growth and liver lipids of casein-fed rats incubated in the presence of glucose and lipid.

The effect of casein that has reacted with glucose and/or lipid on the growth and hepatic lipids of rats was studied. A mixture of casein-ethyl linoleate-glucose was kept at 50 degrees C and RH 80.4% for 14 days and defatted with ethyl ether and acetone. When the casein that had reacted with glucose and lipid was fed at at 10% dietary level for 14 days, the growth of rats was markedly depressed. Not only levels of hepatic lipids but also of plasma lipids were specifically modified. The accumulation of hepatic lipids was primarily due to the increase in triglyceride. When casein was reacted with glucose alone, similar but considerably lesser changes in the growth and liver lipid components were observed. These data indicate that casein characteristically deteriorates with glucose and/or lipid, but the effect of oxidation of the latter is very remarkable.

Animals↗
PubMed1979

Susceptibility of kappa-casein components to various proteases.

In order to clarify the function of the carbohydrate moiety of bovine kappa-casein, kappa-casein components having different carbohydrate contents were prepared by DEAE-cellulose chromatography. Five adsorbed fractions so obtained had an identical peptide chain and contained carbohydrate moieties of increasing size in the order of components P-2, P-3, P-4, P-5 and P-6. The subsceptibility of kappa-casein components, having different carbohydrate contents, to various proteases was examined. kappa-Casein components were subjected to calf rennin [chymosin; EC 3.4.23.4], bovine trypsin [EC 3.4.21.4], alpha-chymotrypsin [EC 3.4.21.1], pronase [EC 3.4.24.4] and human plasmin [EC 3.4.21.7]. The component containing a larger carbohydrate moiety was less susceptible to hydrolysis than the component containing a smaller carbohydrate moiety. Rennin, trypsin, alpha-chymotrypsin and pronase hydrolyzed each component with a different reaction rate. On the contrary, human plasmin hydrolyzed component P-2, but did not hydrolyze component P-5. These results indicate that the carbohydrate moiety of kappa-casein components to various proteases.

Carbohydrate Metabolism↗
PubMed1992

Comparative effect of casein and soybean protein isolate on body fat accumulation in adult rats.

The effect of dietary protein on the body fat accumulation was studied in rats. Adult rats weighing about 300 g were fed 21% protein (casein or soybean protein isolate) and 5% oil diets by pair-feeding for 65 days in Experiment 1. In Experiment 2, only protein and oil contents were changed, 25 and 10%, respectively. Final body weights of the two dietary groups were similar in both experiments, especially in Experiment 2. Total body fat was slightly lower in the soybean protein diet group than in the casein diet group in Experiment 2, only when it was expressed as the percentage against body weight. However, intra-abdominal fat was significantly lower in the soybean protein diet groups than in the casein diet groups in both experiments. Serum lipid levels were greatly lower in the soybean protein diet group than in the casein diet group in Experiment 2 (the data were not available in Experiment 1). The results suggest that dietary soybean protein has the effect to lower the intra-abdominal fat accumulation as compared with casein.

Adipose Tissue↗
PubMed1998

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

Micellar calcium phosphate (MCP) in bovine milk was separated as the complex with casein phosphopeptide (CPP) by the following procedures. Rennet curd obtained from skim milk was suspended in water, the pH was adjusted to 4.6, and the suspension was centrifuged at 1,000 x g. CPP was separated from the precipitated casein by tryptic hydrolysis and ethanol precipitation. The supernatant, which contained calcium and inorganic phosphate liberated from casein micelles by acidification, and CPP were mixed; the pH was adjusted to 6.7; and then the solution was lyophilized. From 1 L of skim milk, 3.16 g of the MCP-CPP complex was obtained. The dried MCP-CPP complex was easily dissolved in water and contained 12.7% calcium, 0.3% magnesium, 3.4% inorganic phosphorous, and 2.2% organic phosphorous. No crystal structure of hydroxyapatite was shown in the MCP-CPP complex by the X-ray diffraction analysis, although the pattern of NaCl crystal was observed. The X-ray diffraction pattern of commercial whey mineral, which was prepared by precipitation at alkaline pH from rennet whey, was similar to that of hydroxyapatite. 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. The MCP-CPP complex was also separated from commercial rennet casein. The method for the separation of MCP-CPP complex described above can be applied to the large-scale preparation.

Animals↗
PubMed1997

A competitive enzyme-linked immunosorbent assay for detection of bovine milk in ovine and caprine milk and cheese using a monoclonal antibody against bovine beta-casein.

A competitive ELISA (enzyme-linked immunosorbent assay) was performed to detect and quantify bovine milk in ovine and caprine milk and cheese using a monoclonal antibody (AH4 MAb) against bovine beta-casein. Ovine or caprine milk and cheese containing bovine milk were added simultaneously with the AH4 MAb to the wells of a microtiter plate that had been previously sensitized with commercial bovine beta-casein. The bovine caseins in milk or cheese samples compete with the bovine beta-casein bound to the plate for the AH4 MAb binding sites. Further immunorecognition of AH4 MAb bound to the bovine beta-casein immobilized onto the plate was attained with rabbit anti-mouse immunoglobulin conjugated to peroxidase. Subsequent enzymic conversion of the substrate showed clear differences in absorbance values during assay of mixtures of ovine and caprine milk and cheese containing various amounts of bovine milk. The competitive ELISA developed in this work allows the quantitative detection of bovine milk in ovine and caprine milk and cheese samples in the range of 0.5 to 25% of substitution.

Animals↗
PubMed1999

A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity.

The Interferon Regulatory Factors (IRFS) play an important role in the transcriptional control of growth regulatory and immunoregulatory genes. The inducibility and availability of IRF-1 and IRF-2 are influenced by external stimuli, such as virus infection or interferon treatment. In the present study, we sought to examine the potential modulatory role of phosphorylation on IRF-1 transcriptional activity. During the purification of IRF recombinant proteins, a kinase activity copurified with IRF-1 (and IRF-2) from baculovirus infected Sf9 insect cell extracts, but not from E. coli extracts. The kinase activity was also identified in Jurkat T cells, specifically interacted with IRF proteins in GST affinity chromatography, and phosphorylated IRF-1 with high specificity in vitro. Using an in gel kinase assay with recombinant IRF-1 as substrate, two molecular weight forms of the kinase (43 and 38 kDa) were identified. Biochemical criteria identified the kinase activity as the alpha catalytic subunit of casein kinase II (CKII). Furthermore, far western analysis of protein-protein interactions demonstrated that casein kinase II directly interacted with IRF-1 protein. Deletion mutation analysis of IRF-1 revealed that IRF-1 was phosphorylated at two clustered sites, one located between amino acids 138-150, the other in the C-terminal acidic activation domain between amino acids 219-231. Cotransfection studies comparing wild type and point mutated forms of IRF-1 demonstrated that mutations of the four phosphoaceptor residues in the C-terminal transactivation domain, significantly decreased transactivation by IRF-1, indicating that casein kinase II may be involved in the regulation of IRF-1 function. Strikingly, the casein kinase II clusters in IRF-1 resemble the sites identified in the C-terminal PEST domain of IkappaBalpha. The present experiments, together with previously published studies with IkappaBalpha, c-Jun and other proteins, indicate a broad role for casein kinase II phosphorylation in the regulation of transcription factor activity.

Blotting, Western↗
PubMedDate not supplied

[Analysis of DNA polymorphism of cluster genes in cattle: casein genes and major histocompatibility complex (MHC) genes].

The PCR-analysis method has been used to study polymorphism of casein genes (k- and b-caseins) and genes of class of basic histocompatibility complex (DRB and DQB BoLA) in some cattle breeds. Genotyping of k-casein locus has been carried out using analysis of protein polymorphism and DNA polymorphism. It is shown that both methods give identical results and can be used for this purpose, but the PCR-analysis method is more informative. A new allele of k-casein gene (k-Cn F) has been revealed and sequenced using the above method. While analyzing DNA-polymorphism of 5'-nontranslated region of b-casein gene two previously non-described polymorphic sites for restrictase Hinf I are found which occur only in animals of "zebu-like" breed. The high level of polymorphism of bl-domain of gene DRB is shown: polymorphism of bl-domain was revealed already at the level of electrophoretic analysis of PCR-amplification products. For 5'-nontranslated domain gene DQB the polymorphism level was much lower and manifested itself during restriction analysis of amplified fragments.

Amino Acid Sequence↗
PubMed2004

Protection against methotrexate toxicity by a soybean protein- and omega-3 fatty acid-containing diet: comparative study with a casein-containing diet.

Effects of two clinically used liquid diets on toxicity and antitumor activity of methotrexate (MTX) were investigated in Sprague-Dawley (SD) rats and tumor-bearing mice, respectively. Diets tested were commercially available formulas enriched either with soybean and omega-3 fatty acids or with casein. The soybean-containing diet offered significant protection against MTX toxicity in rats compared with the casein-containing diet, completely alleviating MTX-induced anorexia, diarrhea, and weight loss, when ingested as the sole diet and fed 7 days prior to and 7 days following intraperitoneal MTX injection. As a result, 90% of rats were alive on soybean-containing diet while all rats were dead on casein-containing diet. Histologic examination of the small intestine of MTX-treated rats revealed that the soybean-containing diet significantly prevented loss of mucosal villus tips compared to the casein-containing diet. Pharmocokinetic examination indicated that plasma MTX concentrations were similar for rats in the two diet-defined groups. No significant differences were observed between diets in survival of mice injected with L1210 mouse leukemia cells and subsequently with MTX. Thus the soybean-containing diet appeared to be superior to the casein-containing diet in preventing gastrointestinal toxicity while preserving antitumor activity. A soybean diet enriched in omega-3 fatty acids may be a useful adjunct to MTX treatment of human cancers.

Animals↗