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PubMed2003

Characterization of equine cDNA sequences for alphaS1-, beta- and kappa-casein.

Here we report the entire cDNA sequences for equine alphaS1-, beta- and kappa-casein. Based on interspecies comparison, nine exons were found in equine beta-casein and five in kappa-casein. In equine alphaS1-casein cDNA the exon 5 was missing, which resulted in the total of 18 exons instead of 19 theoretically possible exons in alphaS1-casein cDNA. Comparison of DNA sequences representing exon 5 in other species with corresponding equine genomic region confirmed the presence of cryptic exon in horse genomic DNA. Equine alphaS1-casein mRNA was present in three forms in the lactating mammary gland and we showed that the two shorter forms were produced by skipping either the exon 8 or exon 15. In horse, as in some other mammals, beta- and kappa-casein are considerably more conserved (sequence identity 53% to 59% and 57% to 67%, respectively) than alphaS1-casein which appears as the most variable casein among species (sequence identity 40% to 54%). Interestingly, horse caseins resemble human much more than bovine caseins which may also explain the high dietetic value of mares' milk.

Alternative Splicing↗
PubMed1976

Quantitation of casein messenger ribonucleic acid sequences using a specific complementary DNA hybridization probe.

Two highly purified rat casein mRNA fractions were used as templates to synthesize complementary DNA (cDNA) hybridization probes using RNA-directed DNA polymerase isolated from avian myeloblastosis virus. Both of the probes selectively hybridized to RNA isolated from lactating mammary tissue, but not to poly(adenylic acid)-containing rat liver RNA. An analysis of the kinetics of hybridization of the cDNA derived from the 15S casein mRNA (cDNA12S) with their individual mRNA templates indicated that greater than 90% hybridization occurred over a R0t range of one and one-half logs with R0t 1/2 values of 0.0023 and 0.0032 mol s l.-1, respectively. Compared with the total RNA isolated from lactating mammary tissue, these values represented a 166- and 245-fold purification, respectively, of these individual mRNA fractions. Using the 15S casein mRNA as a template, two probes of different lengths and specific activities were synthesized. The deoxyribonucleotide and mRNA concentrations and the temperature of incubation were optimized to obtain either a high specific activity cDNA probe, 330 nucleotides long, which represented approximately 25% of the mRNA or a lower specific activity preparation containing some complete cDNA copies, 1300 nucleotides in length. The Tm of the longer cDNA15S-15S mRNA hybrid was 88.5 degrees C, while that of the short cDNA15S-RNA hybrid was 82.5 degrees C. Following this initial characterization, the cDNA15S probe was utilized for three separate determinations: (1) Analysis of the sequence divergence between mouse and rat casein mRNAs. It was observed that the rate of hybridization of heterologous rat cDNA15S-mouse casein mRNA was only 20% that of the homologous rat cDNA15S-rat casein mRNA hybridization. The resulting heterologous hybrid displayed approximately 17% mismatching compared with the homologous hybrid. (2) Determination of the gene dosage for casein mRNA in normal and malignant mammary cells. In this study, an analysis of the kinetics of hybridization of the high specific activity cDNA15S probe with an excess of DNA isolated from lactating mammary tissue, carcinogen-induced mammary tumors, or rat liver indicated that casein mRNA was transcribed from the nonlification or deletion was observed during tumor formation or the process of mammary differentiation. (3) Quantitation of casein mRNA sequences during normal mammary gland development. RNA excess hybridizations were performed using RNA extracted from either pregnant, lactating, or regressed rat mammary tissue. The concentration of casein mRNA molecules/alveolar cell was found to increase 12-fold from 5 days of pregnancy until 8 days of lactation and then declined to approximately 2% of the maximal level of 79 000 molecules/cell by 7 days after weaning. A coordinate increase was observed in casein mRNA sequences detected by cDNA hybridization and mRNA activity measured in a cell-free translation assay.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed2001

Separation and determination of denatured caseins by hydrophobic interaction chromatography Part II. Method validation and applications.

A method recently described for the separation of denatured alpha-, beta- and kappa-caseins by hydrophobic interaction chromatography was validated by the analysis of reference skim milk powder (BCR-063R) certificated for total nitrogen content. The method is based on fast and easy solubilization of commercial and real samples by 4.0 M guanidine thiocyanate and elution on a TSK-Gel Phenyl-5PW column (TosoHaas) in the presence of 8.0 M urea in the mobile phase. No preliminary precipitation or separation of the casein fraction is required. A linear relationship between the concentration of casein and peak area (UV absorbance detector at 280 nm) was obtained over the concentration range 0.5-60 microM. The detection limits for alpha-, beta- and kappa-caseins ranged between 0.30 and 0.65 microM. The precision of the method was evaluated; the relative standard deviation for alpha-, beta- and kappa-casein determination ranged between 2.2 and 2.7% for standard solutions and between 3.5 and 6.2% for real sample solutions. The mean casein content found in 10 aliquots of BCR-063R calculated with respect to the total protein content (estimated on the basis of certified total nitrogen content) was 79.1+/-2.7%. Results of linear fitting of standard additions data for alpha-, beta- and kappa-caseins to BCR-063R were compared with linear fitting of alpha-, beta- and kappa-casein calibration data. The method was applied to commercial caseins and to 31 real, raw samples [processed cow's milk (pasteurised, UHT-treated), follow-up milk powders, cream, cheeses, casein-free infant formulae, cookies for babies containing milk proteins] with the aim of showing the wide applicability of the method in order to determine alpha-, beta- and kappa-caseins.

Animals↗
PubMed2003

Anti-atherogenic effect of soya and rice-protein isolate, compared with casein, in apolipoprotein E-deficient mice.

Our objective was to determine whether dietary plant proteins such as soya-protein isolate (SPI) and rice-protein isolate (RPI) compared with animal proteins, such as casein, could afford beneficial effects on atherosclerosis development in apolipoprotein E-deficient mice. In experiment 1, male and female mice were fed on a purified diet containing either casein, SPI or RPI for 9 weeks. The en face lesion area in the aorta (P<0.05) and the lesion size in the aortic root (P<0.05) in mice fed the casein-based diet were greater than those in the SPI or RPI groups. The plant protein groups had an increased concentration of serum l-arginine (P<0.05) and NO metabolites (NO2 plus NO3) (P<0.05) than did the casein group. The inhibitory effect of the plant proteins on the lesion formations was unrelated to gender and total serum cholesterol. In experiment 2, the l-arginine and l-methionine contents were the same in the l-arginine-supplemented casein-based and SPI-based diets, and between the l-methionine-supplemented SPI-based and the casein-based diets. Male mice were fed on the diets for 15 weeks. There were no significant differences in the en face lesion area and the lesion size between the casein group and the l-arginine-supplemented group, although the serum l-arginine (P<0.05) and NO2 plus NO3 (P<0.05) concentrations in the supplemented group were higher than those in the casein group. There were no significant effects of l-methionine supplementation on the lesion formations. In experiment 3, male mice were given the casein-based diet or the l-arginine-supplemented casein-based diet together with water or water containing an NO synthesis inhibitor for 9 weeks. When given the casein-based diet, the inhibitor drinking, compared with water drinking, resulted in a reduction of the serum NO2 plus NO3 concentration (P<0.01) and an increase in the en face lesion area (P<0.05) and the lesion size (P<0.01). When given the l-arginine-supplemented diet, the inhibitor drinking, compared with water drinking, resulted in no increase in the lesion area and size. These results demonstrate anti-atherogenic potentials of SPI- as well as RPI-derived proteins, but their l-arginine and l-methionine contents were not sufficient enough to explain the underlying mechanism(s).

Animals↗
PubMed1989

Hepatic cysteine sulfinic acid decarboxylase activity in rats fed various levels of dietary casein.

A series of experiments was conducted to examine the effects of dietary protein intake on hepatic cysteine sulfinic acid decarboxylase (EC 4.1.1.29) activity and urinary taurine excretion. When rats were fed diets containing 18, 30, 45 or 60% casein for 1 wk, hepatic cysteine sulfinic acid decarboxylase activity (CSAD) decreased in a progressive and significant manner. Enzyme activity in rats fed a 60% casein diet was 25% of the activity measured in rats fed 18% casein. The time course of the change in CSAD activity was examined in rats fed a 60% casein diet. Within 24 h of switching rats from a moderate (18% casein) to high (60% casein) protein diet, enzyme activity decreased by 50% and continued to decline in rats fed the high protein diet for 7 d. The observed decrease in enzyme activity was reversed when rats were refed the 18% casein diet. The half-life of CSAD was calculated to be 2 and 7 d during the diet switch from 18 to 60% casein and from 60 to 18% casein, respectively. The change in enzyme activity was evident after a single high protein meal. In contrast to CSAD activity, urinary taurine excretion increased 140-fold within 2 d of switching rats from an 18 to 60% casein diet. Upon refeeding of the 18% casein diet taurine excretion rapidly decreased. These findings indicate that CSAD responds in a rapid and reversible manner to dietary protein.

Animals↗
PubMed1999

Consumption of casein instead of soybean protein produces a transient rise in the concentration of sphingomyelin in VLDL in rats.

In rats fed cholesterol-rich diets, dietary casein vs. soybean protein raises VLDL cholesterol concentrations. Because sphingomyelin may be an essential, structural component of VLDL, we tested whether casein feeding would raise VLDL-sphingomyelin. Rats were fed cholesterol-rich semipurified diets containing either soybean protein (35 g/100 g) or casein for up to 21 d. Consistent with previous work, casein consumption increased hepatic and VLDL cholesterol concentrations. Dietary casein also significantly raised the amount of sphingomyelin in the VLDL fraction, but this effect was transient. Casein feeding transiently lowered LDL- and HDL-2-sphingomyelin concentrations. We suggest that an increase in hepatic VLDL secretion after casein consumption imposed an increased demand for sphingomyelin in the liver. The activity of key enzymes of sphingomyelin synthesis, i.e., serine palmitoyltransferase, phosphatidylcholine:ceramide phosphocholinetransferase and phosphatidylethanolamine:ceramide phosphoethanolaminetransferase and sphingomyelin degradation, i.e., acid sphingomyelinase, were enhanced and depressed, respectively, by casein consumption. Again these effects were transient. Thus, these data indicate that the extra sphingomyelin needed after short-term casein feeding came about through enhanced rates of biosynthesis and reduced rates of degradation in the liver. In addition, plasma transfer of sphingomyelin from HDL-2 to VLDL might have contributed to the increase in VLDL sphingomyelin in the casein-fed rats. This study shows that dietary casein vs. soybean protein transiently influences sphingomyelin metabolism in rats.

Animals↗
PubMed1981

Isolation and properties of human kappa-casein.

Human kappa-casein was isolated from human whole casein by gel filtration with Sephadex G-200 and hydroxylapatite chromatography in the presence of sodium dodecyl sulfate (SDS). The kappa-casein was calcium-insensitive and did stabilize human beta-casein and bovine alpha s1-casein against precipitation by calcium ions. Formation of micelles from human beta- and kappa-caseins, and calcium ions was confirmed by electron microscopic observation. On SDS-polyacrylamide gel electrophoresis (SDS-PAGE), a single band was obtained. The formation of para-kappa-caseins by chymosin was confirmed by SDS-PAGE. Two para-kappa-caseins with apparent molecular weights of 13,000 and 11,000 appeared. The molecular weight of intact human kappa-casein was estimated to be approximately 33,000. The human kappa-casein contained about 40% carbohydrate (15% galactose, 3% fucose, 15% hexosamines, and 5% sialic acid) and 0.10% (1 mol/mol) phosphorus. Its amino acid composition was similar to that of bovine kappa-casein except for serine, glutamic acid, and lysine contents.

Amino Acids↗
PubMed1987

Developmental changes in rat hepatic casein kinases 1 and 2.

Cytosolic histone kinase and casein kinase activities varied considerably in the late fetal and postnatal periods of liver development. Both activities showed a maximum at day 21 of gestation and decreased at birth to values close to those of adult rats. The changes in total casein kinase activity were due to variations of casein kinase 1 and casein kinase 2. Similarly the activities of both the cyclic-AMP-dependent protein (histone) kinase and the cyclic-AMP-independent histone kinase varied during development. Besides the changes in total activity, the affinity of casein kinases 1 and 2 for casein also varied in fetal and postnatal development. The Km values of casein kinase 2 increased from day 18, reached a maximum at day 20 of gestation and then started to decrease until one day after birth. In contrast the Km values of casein kinase 1 decreased from day 18, reached its lowest value at day 21 of gestation and attained values similar to those in the adult at the day of birth. Changes in this parameter were also observed when insulin (3 IU/kg) was administered by intraperitoneal injection to one-day-old rats. The Km values of casein kinase 1 decreased while those of casein kinase 2 increased after administration of this hormone. On the other hand, the Km values for ATP of casein kinases 1 and 2 as well as their apparent molecular masses and sensitivity to heparin and GTP did not significantly change during ontogeny of rat liver.

Aging↗
PubMed1993

Differential effect of brefeldin A on phosphorylation of the caseins in lactating mouse mammary epithelial cells.

The major milk proteins, the caseins, contain multiple phosphorylation sites. Phosphorylation of the caseins is necessary to allow Ca2+ binding and aggregation of the caseins to form micelles. We have followed the phosphorylation of the caseins in isolated acini from lactating mouse mammary gland. Incubation of mammary cells with [32P]orthophosphate revealed that phosphorylation of newly synthesised caseins was complete within 20 minutes of synthesis. Extensive secretion of alpha-, beta- and gamma-caseins occurred over a 2 hour period. Activation of the regulated secretory pathway using ionomycin over the last hour resulted in a preferential increase in secretion of alpha- and gamma-caseins. Brefeldin A (BFA) inhibited protein secretion and synthesis in mammary cells in prolonged incubations. An examination of short-term treatments with BFA on 32P incorporation into the caseins revealed a differential effect of BFA in which the drug inhibited phosphorylation of beta- and gamma- but not alpha-caseins. These results suggest that phosphorylation of alpha-casein normally occurs in Golgi cisternae whereas that of beta- and gamma-caseins occurs in the trans-Golgi network. Phosphorylation of specific secretory proteins may, therefore, occur in different Golgi compartments.

Animals↗
PubMed2001

Gastric proteinase digestion of caseins in newborn pups of the mouse.

Casein micelles of mouse milk consist of alpha-, beta-, gamma-, and kappa-caseins. By digestion with alkaline phosphatase, they were separated as an independent band by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). The compositions of alpha-, beta-, gamma-, and kappa-caseins were 24.3, 25.1, 9.4, and 41.2% in colostrum, and 36.8, 15.6, 11.9, and 35.7% in mature milk, respectively. Zero-day-old pups were allowed to access either colostrum or mature milk, and the aggregated milk in the stomach was analyzed by SDS-PAGE. Caseins in colostrum were digested more rapidly and efficiently than those in mature milk. Among the seven peptides present in the aggregated caseins, four peptides were colostrum-specific and derived from alpha- and gamma-caseins. It was expected that colostrum-specific and soluble peptides were generated from alpha- and gamma-caseins through gastric proteinase digestion. Amino acid sequence analysis and the pH of the aggregated milk suggested that caseins in the stomach were digested by a chymotrypsin-like proteinase. Caseins in colostrum were different from those in mature milk, with respects to the casein composition as well as the gastric proteinase sensitivity. It is concluded that the lactating mice on the day of parturition supply particular caseins to their young.

Animals↗
PubMed2002

Casein interactions studied by the surface plasmon resonance technique.

Surface plasmon resonance technique was investigated for the first time to study the apparent hydrophobicity and association properties of the major bovine caseins: alpha(s)-(alpha(s1)- and alpha(s2)-caseins in a 4:1 proportion), beta-, and kappa-caseins. The apparent hydrophobicities of the caseins were evaluated by a new method based on the binding level of casein on a hydrophobic sensor chip, and kinetic and equilibrium affinity constants were determined for the following casein interactions: alpha(s)/alpha(s), alpha(s)/beta, alpha(s)/kappa, beta/beta, and beta/kappa, using a sensor chip modified with covalent immobilized caseins. The study by surface plasmon resonance technology of these casein interactions under different conditions (pH, ionic strength, calcium concentration, chemical modification) demonstrated that, at neutral pH, electrostatic repulsive forces play an important role since an increase in ionic strength of the medium resulted in a stronger interaction. When charge repulsions were reduced by either acidification, increase in ionic strength, or dephosphorylation, casein interactions were reinforced, presumably due to weak attractive forces. Moreover, in this molecular model, we showed that addition of calcium greatly increased the binding response between the most phosphorylated caseins and that the added calcium (2 mM) participated directly in the formation of bridges between the phosphate groups of the casein molecules.

Adsorption↗
PubMed2003

Effects of casein and glucose on responses of cows fed diets based on restrictively fermented grass silage.

This study was conducted to investigate whether well fed dairy cows given restrictively fermented grass silage diet will respond to incremental glucose and amino acid supply at early stage of lactation. Four rumen-cannulated Finnish Ayrshire cows were used in a 4 x 4 Latin square experiment with 14-d periods. The cows were fed good quality restrictively fermented grass silage ensiled with a formic acid additive for ad libitum intake. A concentrate mixture consisting of barley (85%) and solvent extracted rapeseed meal (11.4%) was given at a rate of 9 kg/d. The four treatments were continuous abomasal infusions of water (control), casein 300 g/d, glucose 300 g/d, and casein 300 g/d + glucose 300 g/d. The infusions had only minor effects on feed intake, diet digestibility, or rumen fermentation pattern. Both casein and glucose infusions increased milk, protein and lactose yields the effects being partly additive on the combined infusion. Infused casein increased milk protein and urea as well as plasma urea concentrations. Both casein and glucose tended to increase plasma glucose concentration. Casein increased arterial plasma concentrations of essential amino acids (EAA), branched-chain AA (BCAA), and total AA (TAA). Both casein and glucose, although glucose usually less than casein, increased arteriovenous differences of EAA, nonessential AA, BCAA, and TAA. Extraction efficiencies of AA were higher for glucose than for casein. Mammary plasma flow was at highest on the control diet, but reduced owing to infused nutrients, the reduction being less with combined rather than separate infusions of casein and glucose. Based on the partly additive increases in milk production parameters and changes in plasma metabolites, it is suggested that glucose alone increased milk protein yield by sparing AA from hepatic utilization, while casein increased both supply of AA and glucose. It was concluded that cows at early stage of lactation fed diets comprising of restrictively fermented grass silage and a cereal-based concentrate suffer from both limited AA and glucose supplies.

Abomasum↗
PubMed2006

Casein breakdown in terrincho ovine cheese: comparison with bovine cheese and with bovine/ovine cheeses.

Terrincho cheese is an uncooked, pressed cheese made from raw whole ovine milk from the "Churra da Terra Quente" breed. It requires a minimum ripening time of 30 d. A detailed evaluation of the effect of ripening time on the breakdown of the casein fractions, along with the formation of major breakdown products of casein hydrolysis, was monitored by HPLC to contribute to a more complete characterization of this product. In 30-d-old cheeses, only 20% of alpha(S1)-casein remained intact; the beta-casein fraction was more resistant to hydrolysis. The ripening time of Terrincho cheese can be predicted using 2 variables of normalized peak areas of alpha(S1)-casein and alpha(S1)-I peptide, and a constant; the estimation error is 2.5 d. The pH 4.3-insoluble fraction of Terrincho and cheeses manufactured with bovine milk and with ovine milk combined with 2 levels of bovine milk (10 and 20%) revealed different chromatographic and electrophoretic profiles, especially the alpha(S1)-casein fraction. Similar proteolysis progress was observed, particularly in the percentage of casein fraction degradation. However, using both analytical methods, the detection of 10% bovine milk at 30 d of ripening was no longer possible as result of alpha(S1)-casein hydrolysis. The discriminate analysis applied to HPLC data indicated that at 30 d of ripening, differences between the casein fractions of Terrincho cheese and mixture cheeses were mainly from beta1-casein content. The function thus obtained was able to correctly classify all the samples according to cheese type. Using the descriptive sensory profile, Terrincho cheese at 30 d of ripening could be distinguished from bovine and mixture cheeses owing to its higher fracturability and adhesiveness and lower elasticity and hardness, which correlated with its lower total casein content.

Animals↗
PubMed1992

The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate.

Artificial casein micelles were formed with whole human casein at 20 mM calcium, 17 mM phosphate, and 10 mM citrate. The casein micelles disaggregated by 6 M urea were separated by high performance gel chromatography on a TSK-GEL G4000SW column into crosslinked and monomeric fractions. When the crosslinked casein fraction was analyzed by high performance ionexchange chromatography on a TSK-GEL DEAE-5PW column, a small peak, representing the 3-P component of human beta-casein, and distinct peaks of the 4-P and 5-P components were found. Artificial casein micelles were formed from mixtures of each purified component of human beta-casein and bovine kappa-casein, disaggregated by urea, and separated on a TSK-GEL G4000SW column. The casein aggregates crosslinked by colloidal calcium phosphate were formed in artificial casein micelles of the 3-P and 4-P components. In contrast, no crosslinkage was formed in artificial micelles of the 1-P and 2-P components. The results indicate that at least three phosphate groups are needed for crosslinking of casein by colloidal calcium phosphate.

Animals↗
PubMed1999

Effects of branched-chain amino acids and sodium caseinate on milk protein concentration and yield from dairy cows.

Our study investigated the separate and combined effects of branched-chain amino acids (AA) and sodium caseinate on milk protein concentration and yield. Four Holstein cows (112 d in milk) were abomasally infused with water, branched-chain AA (150 g/d), sodium caseinate (600 g/d), or branched-chain AA plus sodium caseinate (44 and 600 g/d, respectively) according to a 4 x 4 Latin square design with 8-d treatment periods. Cows were fed a dry diet based on alfalfa hay and concentrates for ad libitum intake. The ration was formulated to exceed requirements for metabolizable energy and protein using the Cornell Net Carbohydrate and Protein System. Neither daily dry matter intake (24.2 +/- 0.4 kg/d; X +/- SEM) nor milk yield (32.9 +/-; 0.4 kg/d) was affected by any of the infusion treatments. Infusion of branched-chain AA had no effect on any milk production parameters, despite a 50% increase in their concentrations. Modest increases in milk protein concentration (0.1%) and milk protein yield (62 g/d) resulted from the infusion of sodium caseinate or branched-chain AA plus sodium caseinate. True protein and whey protein concentrations in milk were also marginally increased by infusion of sodium caseinate and branched-chain AA plus sodium caseinate, and infusion of branched-chain AA, sodium caseinate, or both elevated milk nonprotein N content. Plasma urea N concentrations were elevated by the sodium caseinate and branched-chain AA plus sodium caseinate treatments. No treatment effects on other plasma metabolites or hormones were observed. Our results show no benefit of supplementation with branched-chain AA and only modest effects of sodium caseinate on milk protein concentration and yield in well-fed cows.

Abomasum↗
PubMed2000

Effects of graded levels of dietary casein and corn oil on total cholesterol and triacylglycerol in plasma and liver of rats.

With the intention of examining the effects of dietary protein and oil levels on total cholesterol (T-CHOL) and triacylglycerol (TG) concentrations in the plasma and liver, male Wistar rats, weighing about 170 g, were fed diets containing graded levels of casein and corn oil for 2 wk. At the 5, 20, and 30% levels of dietary corn oil, plasma T-CHOL concentrations were generally enhanced in proportion to the rise of dietary casein level, but plasma TG contents were scarcely influenced by the level. At the 8 to 35% casein levels, plasma T-CHOL and TG concentrations were the highest at the 5% corn oil level, followed in order by the 20 and 30% levels of oil. At the 5 and 20% oil levels, hepatic T-CHOL contents were hardly changed at the 8 to 30% casein levels, but enhanced at the 35% casein level. At the 30% oil level, the T-CHOL contents tended to be changed proportionally to casein levels. At all levels of casein, hepatic T-CHOL contents tended to be relatively high at the 30% corn oil, middle at the 20% oil, and low at the 5% one. At each corn oil level, TG contents in the liver tended to be elevated at the 8 to 15% casein levels and highly preserved at the 15 to 25% ones. Then, the raised TG contents declined at the 5 and 20% levels of corn oil and remained constant at the 30% oil. At each casein level, the contents of hepatic TG were generally high at the 30% oil level, followed in order by the 20 and 5% oil levels. These results indicated that plasma and liver T-CHOL concentrations were proportionately enhnaced by the increase in casein level, and plasma TG contents were hardly affected by the level and hepatic TG ones were lowered by relatively lower or higher casein level, and the rise in corn oil level generally reduced plasma T-CHOL and TG concentrations, but raised hepatic ones.

Animals↗
PubMed1991

Principal neurofilament-associated protein kinase in squid axoplasm is related to casein kinase I.

A cytoskeletal extract of pure axoplasm, highly enriched with neurofilaments (ANF), was prepared from the giant axon of the squid. This ANF preparation also contained potent kinase activities which phosphorylated the Mr greater than 400,000 (high molecular weight) and Mr 220,000 squid neurofilament protein subunits. High salt (1 M) extraction of this ANF preparation solubilized most of the neurofilament proteins and kinase activities and gel filtration on an AcA 44 column separated these two components. The neurofilaments eluted in the void volume of the column while the kinase activities eluted in the 17-44-kDa range of the column. Two major kinase activities were measured in this peak of activity. One of these strongly phosphorylated the phosphate acceptor peptide Leu-Arg-Arg-Ala-Ser-Leu-Gly (Kemptide) and was completely inhibited by the selective inhibitor of cAMP-dependent kinase Thr-Thr-Tyr-Ala-Asp-Phe-Ile-Ala-Ser-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile- NH2 (Wiptide). Since addition of cAMP did not stimulate activity, this suggested that this kinase was a free catalytic subunit of cAMP-dependent kinase associated with the neurofilaments. The second kinase activity most effectively phosphorylated alpha-casein, and this activity was not affected by Wiptide. The alpha-casein phosphorylating activity (ANF kinase) was the principal activity responsible for neurofilament protein phosphorylation, and was not inhibited by various inhibitors against second messenger regulated kinases, suggesting it was related to the casein kinase family. Four lines of evidence indicate ANF kinase was similar to casein kinase I. These were: 1) the apparent molecular weight determined by gel filtration and the chromatographic elution profile on phosphocellulose column corresponded to casein kinase I; 2) heparin, an inhibitor of casein kinase II at 2-5 micrograms/ml, stimulated both ANF kinase and purified casein kinase I at these concentrations, while CKI-7, a relatively selective inhibitor of casein kinase I, inhibited ANF kinase in a comparable dose-response fashion; 3) purified casein kinase I strongly phosphorylated both ANF protein subunits (like ANF kinase) whereas casein kinase II was relatively ineffective; and 4) tryptic peptide maps of the HMW and Mr 220,000 neurofilament proteins after phosphorylation by ANF kinase or purified casein kinase I showed similar 32P-peptide patterns.

Animals↗
PubMed1994

Preferential recognition of primary protein structures of alpha-casein by IgG and IgE antibodies of patients with milk allergy.

We studied the binding activities of IgE and IgG antibodies in patients with allergy to cow milk proteins, against different alpha-casein preparations: alpha-casein treated with urea, hydrochloric acid, sodium hydroxide, or sodium dodecyl sulfate (SDS); or heat-denatured alpha-casein. The binding activities of IgE and IgG antibodies to these denatured alpha-casein preparations were compared with those to native alpha-casein. The binding activities of IgE and IgG antibodies to these denatured alpha-casein preparations were similar to those to native alpha-casein although the binding activities of IgG antibodies to these denatured alpha-casein preparations were relatively heterogeneous compared with those of IgE antibodies. Since modifications of alpha-casein did not alter the ability of alpha-casein to react with these antibodies, IgE and IgG antibodies to alpha-casein in sera from patients with allergy preferentially bind to the antigenic determinants associated with primary protein structures.

Allergens↗