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 379 records · Page 21Linked to original sources
PubMed2001

Processing and localization of bovine beta-casein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette.

We have examined the processing and subcellular localization of a chimeric gene consisting of the bovine milk protein, beta-casein, under the control of a soybean seed lectin promoter and its 32 amino acid signal sequence in the seeds of transgenic soybean plants. The beta-casein expressed in developing soybean seeds is a doublet with apparent molecular weight slightly smaller than the bovine beta-casein and expression of the protein was highest in immature cotyledons. The casein proteins were purified from the immature soybean seeds by immunoaffinity chromatography and were analyzed by two-dimensional gel electrophoresis, blotting, and amino terminal sequencing. The N-terminal sequences of both of the doublet soybean casein polypeptides were identical to the N-terminal sequence of the bovine beta-casein indicating that the 32 amino acid lectin signal sequence was cleaved precisely from the chimeric protein in developing soybean seeds. Analysis of the purified soybean beta-casein polypeptides by mass spectrometry (MALDI-MS) showed that they are not phosphorylated. Absence of added phosphate groups is the cause of the size difference between the soybean beta-casein and native bovine beta-casein protein. Immunolocalization experiments showed that the casein protein was found in the protein storage vacuoles (PSV) in developing and mature soybean seeds. The precise removal of the 32 amino acid lectin amino terminal sequence from the chimeric lectin-casein fusion suggests that the lectin expression cassette can be used for production of pharmaceutical or other recombinant proteins of added value in the developing soybean seed.

Journal Article↗
PubMed1990

Phosphate groups as substrate determinants for casein kinase I action.

Phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase has been shown to enhance subsequent phosphorylation by casein kinase I (Flotow, H., and Roach, P. J. (1989) J. Biol. Chem. 264, 9126-9128). In the present study, synthetic peptides based on the sequences of the four phosphorylated regions in muscle glycogen synthase were used to probe the role of substrate phosphorylation in casein kinase I action. With all four peptides, prior phosphorylation significantly stimulated phosphorylation by casein kinase I. A series of peptides was synthesized based on the NH2-terminal glycogen synthase sequence PLSRTLS7VSS10LPGL, in which phosphorylation at Ser7 is required for modification of Ser10 by casein kinase I. The spacing between the P-Ser and the acceptor Ser was varied to have 1, 2, or 3 intervening residues. The peptide with a 2-residue spacing (-S(P)-X-X-S-) was by far the best casein kinase I substrate. When the P-Ser residue at Ser7 was replaced with P-Thr, the resulting peptide was still a casein kinase I substrate. However, substitution of Asp or Glu residues at Ser7 led to peptides that were not phosphorylated by casein kinase I. Phosphorylation of one of the other peptides showed that Thr could also be the phosphate acceptor. From these results, we propose that there are substrates for casein kinase I for which prior phosphorylation is a critical determinant of protein kinase action. In these instances, an important recognition motif for casein kinase I appears to be -S(P)/T(P)-Xn-S/T- with n = 2 much more effective than n = 1 or n = 3. Thus, casein kinase I may be involved in hierarchal substrate phosphorylation schemes in which its activity is controlled by the phosphorylation state of its substrates.

Amino Acid Sequence↗
PubMed1981

[Chemical modification of proteins. 7. Effect of succinylation on some physico-chemical and functional properties of casein].

Succinylation of amino groups of the casein complex results in a spontaneous dissociation of the protein into low-molecular 1.8-S components. Succinylated samples of casein are characterized by a higher electrophoretic mobility of the components in alkaline mediums and by a lower mobility in acidic buffer systems. The anodic migration in alkaline buffer systems increases depending on the degree of modification. This effect is more pronounced for the beta-casein than for the alpha s-casein fraction. In the potentiometric acid-base titration of the modified casein a hysteresis occurs during the back-titration. Increasing with the degree of modification, this effect points to a more or less strong break-up of the structure (entropy production). The solubility minimum of casein is shifted to lower pH values by succinylation. Samples succinylated to 90 or more per cent of the amino groups are insoluble at pH less than 3.5. Succinylated casein shows at a moderate degree of substitution (approximately equal to 40%) a highly increased water adsorption capacity. The oil adsorption capacity of the protein decreases after succinylation. Amongst the modified casein samples those ones with the highest water adsorption show the highest oil adsorption, too. The emulsifying capacity of low (approximately equal to 20%) succinylated casein samples decreases below the value determined for the unmodified protein. At higher modified samples the emulsifying capacity increases as the degree of succinylation increases. The emulsifying activity and emulsion stability of modified samples are lower than that measured for the parent protein. The foaming capacity of the casein is not improved by succinylation.

Caseins↗
PubMed1991

Stimulation of proliferation and immunoglobulin production of human-human hybridoma by various types of caseins and their protease digests.

We have studied the effect of such milk proteins as caseins, lactalbumin, and lactoglobulin, on proliferation and immunoglobulin production of human-human hybridoma HB4C5 cells. It was found that alpha-, beta-, and kappa-caseins stimulated both proliferation and IgM product ion of human-human hybridoma HB4C5 cells, while the activities of alpha-lactalbumin and beta-lactoglobulin were negligible. To localize the active sites of these caseins, effect of protease treatments on the activities were examined. When caseins were digested with trypsin, casein digests stimulated proliferation of the hybridoma, but not their IgM production. When kappa-casein was digested with chymosin and fractionated to p-kappa-casein and glycomacropeptide, both fragments stimulated proliferation of the cells, but only p-kappa-casein fragment stimulated IgM production. These results indicate that kappa-casein has at least two proliferation stimulating sites and an IgM production stimulating site in the p-kappa-casein region.

Antibodies, Monoclonal↗
PubMed1991

Relationship between naturally occurring human antibodies to casein and autologous antiidiotypic antibodies: implications for the network theory.

Previous studies on human autologous antiidiotypes have been based largely upon analyses of autoimmune disease. We have previously described polyclonal, naturally occurring human autoantibodies directed against antibodies with specificity toward bovine casein in the sera of IgA-deficient humans. In order to define this system more exactly we have not produced two murine monoclonal antibodies directed against bovine milk kappa-casein to use as clonal tools to identify specific antiidiotypes in these human sera. Kappa-casein is an important part of the casein micelle in milk and cheese; in addition to being an important immunogen for man, kappa-casein is known to have conserved amino acid sequence and two antigenic epitopes. Data presented here show that the serum of up to 74% of IgA-deficient and 10% of normal humans have specific autologous antiidiotypes in their serum which bind to monoclonal antibodies directed to bovine kappa-casein. These human antibodies [intact or F(ab)'2] can be blocked from binding to the monoclonal anti-kappa-caseins by pure bovine kappa-casein or the kappa-casein peptide fragment. In contrast to previous studies in autoimmune disease, serum levels of the autoantiidiotypes were directly proportional to the level of IgG antibody to bovine kappa-casein. These observations suggest that continual exposure to a ubiquitous dietary antigen may produce an antigen driven system in which stimulation of both Ab1 and Ab2 occurs in concert.

Adolescent↗
PubMed1979

Isolation and characterization of porcine beta-casein.

Porcine beta-casein was isolated by chromatography on DEAE-cellulose. The protein had a molecular weight of 24 900 as determined by gel filtration on Sephadex G-100 in guanidine-HCl. Its amino acid composition differed from bovine beta-casein especia-ly in respect to serine, alanine and leucine. In common with bovine beta-casein the N-terminal amino acid was arginine; the C-terminal was either alanine or valine, while the C-terminal of bovine beta-casein is valine. At any temperature porcine beta-casein was more sensitive to Ca2+ than bovine beta-casein, while at a fixed Ca2+ concentration porcine beta-casein aggregated at a lower temperature than bovine beta-casein. Porcine beta-casein was susceptible to hydrolysis by calf chymosin but the proteolytic specificity differed from that of calf chymosin on bovine beta-casein.

Amino Acids↗
PubMed1981

Purification and properties of a major casein component of rat milk.

A casein component (C2-casein) was purified by ion-exchange and gel filtration chromatography from rat milk, and the properties of this protein were examined. The molecular weight of C2-casein, as determined by Sepharose 4B gel filtration in 6 M guanidine hydrochloride, was 34 000 +/- 1000. The average hydrophobicity calculated from the amino acid composition showed that C2-casein is a rather hydrophilic protein. The alpha-helix content obtained from optical rotatory dispersion experiments was about 12%. In ultracentrifugation analyses, monomer and polymer peaks of C2-casein were both seen, and the monomer-to-polymer ratio was not affected by changing temperature conditions. C2-casein was precipitated by the presence of 2.5 mM CaCl2, and the precipitability was greatly decreased by the dephosphorylation of the protein. C2-casein was stabilized from Ca2+-dependent precipitation by the addition of another rat casein component (C3-casein) or of bovine kappa-casein.

Amino Acids↗
PubMed1989

Influence of fish protein as compared to casein and soy protein on serum and liver lipids, and serum lipoprotein cholesterol levels in the rabbit.

Serum and hepatic cholesterol and triglyceride levels, and serum lipoprotein cholesterol were investigated in rabbits fed fish protein as compared to casein and soy protein as part of a 20% protein, low fat, cholesterol-free, semi-purified diet. A nonpurified diet was used as a control. After a 28-day experimental period, rabbits fed casein developed hypercholesterolemia compared to those fed the soy protein diet. Serum cholesterol levels of rabbits fed fish protein was intermediate and not different from that of the casein or the soy protein group. However, serum triglycerides were higher in the fish group than in the casein group. Feeding of fish protein resulted in a reduction of hepatic cholesterol compared to casein, indicating no direct relationship between serum and hepatic cholesterol. In addition, fish protein induced a decrease of cholesterol in the low density lipoproteins (LDL) compared to casein and an increase of cholesterol in the high density lipoproteins (HDL) compared to casein and soy protein. Reduction in LDL-cholesterol (LDL-C) and elevation in HDL-cholesterol (HDL-C) caused a 10-fold decrease in the LDL-C/HDL-C ratio of fish protein fed rabbits compared to those fed casein. This ratio was similar to that observed with soy protein which was also lower than the ratio of the casein group. Thus, since the LDL-C/HDL-C ratio has been shown to be a good indicator of the atherosclerosis risk, these results suggest that fish protein, as well as soy protein, may reduce the risk of atherosclerosis in rabbits, compared to casein.

Animals↗
PubMed1996

Effect of dietary casein levels on activation of promutagens in the spiral Salmonella mutagenicity assay. II. Studies with induced rat liver S9.

In the previous study (Mutation Res., this issue), we showed that increased levels of dietary casein as the sole protein source for male F344 rats decreased the ability of the uninduced liver S9s to activate 2-aminoanthracene (2AN) to a mutagen in strain TA98 using the spiral Salmonella mutagenicity assay. No effects of dietary casein levels were noted for the ability of uninduced liver S9s to activate the promutagens aflatoxin B1 (AFB) and benzo[a]pyrene (BAP). In the present study, we have extended this study to include liver S9s induced with either Aroclor 1254, phenobarbital or 3-methylcholanthrene (3MC). S9s were derived from individual male F344 rats fed for 6 weeks on semisynthetic diets containing 8%, 12% or 22% methionine-supplemented casein as the sole source of protein (diets were made isocaloric by adjusting the corn starch content). Rats were housed in large, raised-bed cages by groups of three/diet/inducing agent. S9 activation mixtures were prepared at 5 mg of S9 protein/ml of S9 mix. Slopes from the linear portions of the mutagenicity dose-response curves were analyzed by ANOVA comparisons. Assays used to elucidate the phase I activities of microsomal preparations were cytochrome P-450 content, cytochrome-c reductase activity, flavin-containing monooxygenase activity, 7-ethoxyresorufin O-deethylation (EROD) activity, N-demethylation of benzphetamine, and para-nitrophenol O-deethylation. Phase II activities were assayed by estimating glutathione (GSH) content and measuring the metabolism of 1-chloro-2,4-dinitrobenzene (CDNB) by glutathione S-transferase in cytosolic preparations. None of the phase I or phase II endpoints were significantly affected by dietary casein levels. In general, increasing levels of dietary casein resulted in increased body and liver wet weight and amount of S9 protein. Aroclor-induced S9s from rats fed the 22% or 12% casein diet were most effective at activating AFB, depending on the lot of Aroclor used for induction; these divergent results were replicated with two groups of rats for each lot of Aroclor. The observed differences between Aroclor lots are assumed to arise from variation in the mix of PCB isomers. The Aroclor-induced S9s did not exhibit any casein-related effects for the activation of BAP or 2AN. For 3MC-induced S9s, the 12% casein diets produced S9s with the highest ability to activate AFB and BAP when standardized for protein content. Phenobarbital-induced S9s did not demonstrate any dietary casein-related effects on the activation of the three model promutagens. These results illustrate the complex interaction between dietary levels of casein, enzyme inducing agent and promutagen.

Aflatoxin B1↗
PubMed1983

Catalytic and molecular properties of a highly purified G type casein kinase from bovine lung tissue.

A preparation procedure has been worked out to obtain a highly purified G type (using GTP as well as ATP) casein kinase from large quantities of bovine lung tissue. It included ion-exchange (DEAE and phosphocellulose) and affinity (casein and ATP-Sepharose) chromatography combined with a flocculation step, and yielded an apparently homogeneous preparation with a 16% yield and a purification factor of more than 1400. The purified lung casein kinase used GTP (Km 16 microM) almost as well as ATP (Km 6.7 microM) and exhibited the major catalytic properties of the casein kinase G previously described in bovine adrenal cortex (Cochet, C., Job, D., Pirollet, F. and Chambaz, E.M. (1981) Biochim. Biophys. Acta 658, 191-201). Mg2+ (30-50 mM) and spermine (2 mM) were potent activators of lung casein kinase G activity, whereas the enzyme was inhibited by heparin and quercetin. The purified enzyme underwent self-phosphorylation in the presence of ATP or GTP, serine being the only target amino acid under these conditions, whereas both serine and threonine were phosphorylated by the enzyme in casein. Lung casein kinase G exhibited an apparent molecular weight between 140 000-160 000 upon gel filtration and appeared formed by the association of two different subunits upon SDS-polyacrylamide gel electrophoresis. The two subunits of Mr 38 000 (alpha) and 27 000 (beta) exhibited a 2:1 ratio upon quantitative scanning, suggesting an alpha 3 beta 2 combination in the oligomeric native enzyme structure. Peptide mapping of the two isolated subunits following 125I-labeling and papain digestion did not disclose any common fragment. The casein kinase catalytic activity was found associated with the alpha (38 kDa) enzyme subunit after recovery from gel electrophoresis in the presence of SDS, whereas the 27 kDa (beta) subunit was the major target of the enzyme self-phosphorylation reaction. alpha and beta subunits appeared strongly associated in the oligomeric enzyme and the possible role of the beta subunit in the casein kinase G activity remains to be examined. The purified casein kinase G, which can be obtained by the present procedure, should facilitate the study of the biological significance of this phosphorylation system in the intact cell.

Animals↗
PubMed1993

Antimutagenic effects of casein and its digestion products.

The antimutagenic potential of casein was investigated using several mutagens, including some food-related mutagens, and the Salmonella/microsome and Escherichia coli DNA-repair tests. The effect depended on the type of mutagen and the incubation time of casein with the mutagens. Casein was very effective against benzo[a]pyrene, N-methylnitrosourea and nitrosated 4-chloroindole, and was less effective towards sodium azide and N-nitroquinoline-1-oxide (NQO). Preincubation increased the antimutagenic potential of casein towards NQO. Heating of casein (up to 20 min at 130 degrees C) did not alter its antimutagenic capacity. The effect of pepsin hydrolysis under simulated gastric conditions on the antimutagenic capacity of casein was tested with sodium azide and NQO in the Salmonella/microsome test. The peptides formed were separated by ultrafiltration or by isoelectric precipitation of casein, and were characterized by HPLC size-exclusion and Kjeldahl analysis. The antimutagenic potential of casein increased with pepsin hydrolysis; this increase was due to the peptides formed and might be explained by a better accessibility of casein peptides for interaction with mutagens. The antimutagenic potential of pepsin-hydrolysed casein towards sodium azide was observed over the whole dose-response curve.

Antimutagenic Agents↗
PubMed1986

Interaction of casein with human polymorphonuclear cells.

Attachment of 125I-casein to PMN cells was investigated. Iodination did not decrease the chemotactic effect of casein. 125I-casein binding was increasing toward a maximum reached at about 45 min at 24, and 37 degrees C. At 4 degrees C the binding was proportional to time for 45 min. No saturation was achieved even at 15 mg/ml casein. About 40% of casein remained attached to PMN in a casein-free medium after 60 min, at 37 degrees C. Pretreatment of the cells with trypsin or butanol, or the presence of indomethacin, azide, and PMSF did not affect the binding of casein. The hydrophobic amino acid, leucin counteracted the attachment of casein. Our data show that at chemotactic doses casein is bound specifically to cell membranes by hydrophobic forces. The induction of chemotaxis may be due to micellar casein-membrane lipid complexes.

Adult↗
PubMed2004

Inhibition of heat-induced aggregation of a beta-lactoglobulin-stabilized emulsion by very small additions of casein.

Heat stability has been studied in model systems of oil-in-water emulsions (3 wt.% total protein, 45 vol.% n-tetradecane, pH 6.8, ionic strength 30-50 mM) with pure beta-lactoglobulin (beta-lg) as the main emulsifier. The effect of small additions of sodium caseinate, beta-casein or alpha s1-casein prior to emulsion preparation has been investigated. Samples heated for 3 min at 90 degrees C were monitored with respect to changes in viscosity and particle-size distribution. As expected, the pure beta-lg-stabilized emulsions were susceptible to heat-induced changes. But the replacement of just 1% of the beta-lg by sodium caseinate (0.03 wt.% caseinate in the total emulsion) led to complete elimination of any heat-induced viscosity or particle size increase. These findings show that a very small proportion of casein can inhibit the susceptibility of a beta-lg-based emulsion to heat-induced destabilization. The magnitude of the effect is dependent on the type of casein, with the order of effectiveness being beta-casein>sodium caseinate>alpha s1-casein. This work has potential implications for the development of milk protein-stabilized emulsions of improved shelf life.

Animals↗
PubMed2006

Effect of intrauterine injection of casein on fetal survival in rat: a new pharmacological approach for contraception.

BACKGROUND: The incidental finding of casein as a possible new local pharmacological contraceptive prompted us to assess its validity in an experimental rat model. METHODS: The intrauterine injection of 150 microg of bovine alpha-casein dissolved in 150 microL phosphate-buffered saline (PBS) was performed on one uterine rat horn on days L(5)-L(7), whereas the contralateral horn was used for injection of 150 microL PBS as a control. Intraperitoneal injection of alpha-casein (5 mg/mL, 2 mL/rat) was performed on day L(5). The rats were killed by cervical dislocation on the day L(14). RESULTS: The effect of an alpha-casein on fetal resorption rate was assessed following the unilateral injection of 150 microL of alpha-casein (1 mg/mL in PBS) and compared with the effect obtained following the contralateral injection of 150 microL PBS. The unilateral injection of alpha-casein on day L(5) caused a significant increase in fetal resorption rate as compared with the contralateral uterine horn injected with PBS (p<.00001). The decrease in alpha-casein concentration from 1 to 0.3 mg/mL caused a reduced, but still significant, effect on fetal resorption rate (p<.0001). The injection on days L(6)-L(7) caused a local effect of resorption near the injection site. There was no effect on fetal resorption rate following the injection of alpha-casein intraperitoneally. CONCLUSION: Our data suggest a new pharmacological approach for contraception, based on local intrauterine effect of alpha-casein in an experimental rat model. The exact mechanism of action related to casein should be further studied.

Animals↗
PubMed2003

The first intron of the murine beta-casein gene contains a functional promoter.

Caseins are the major milk proteins in most mammals. Together with calcium and phosphate they form the casein micelle. The corresponding casein genes are clustered in mammalian genomes and their expression is coordinately regulated with regard to developmental and tissue specificity. Casein gene promoters are responsive to lactogenic hormones, cell-matrix, and cell-cell interactions. Transcriptional enhancer elements are found in the 5(') upstream regions of casein genes but have also been detected in the first intron of the bovine beta-casein gene. We show here that the first intron of the murine beta-casein gene has three discernible functions. First, transcriptional enhancer elements present in the intron increase the basal activity of the beta-casein promoter. In addition, these intronic enhancer elements augment the induction of the beta-casein promoter by lactogenic hormones. Finally, we demonstrate that the first intron of the murine beta-casein gene contains a functional promoter.

Animals↗
PubMed2003

Separation and determination of denatured alpha(s1)-, alpha(s2)-, beta- and kappa-caseins by hydrophobic interaction chromatography in cows', ewes' and goats' milk, milk mixtures and cheeses.

Caseins alpha(s1)-, alpha(s2)-, beta- and kappa- from raw cows', ewes' and goats' milk were separated and determined by hydrophobic interaction chromatography (HIC) by using a Propyl column (Eichrom) in the presence of 8.0 M urea in the mobile phase. The method is based on fast and easy solubilization of real raw samples by 4.0 M guanidine thiocyanate followed by the HIC analysis, without any preliminary precipitation or separation of the casein fraction. Elution conditions have been optimized by analyzing commercial single bovine standard caseins and their mixture. In the optimized chromatographic conditions the four casein fractions were separated in less than 45 min. A linear relationship between the concentration of casein and peak area (UV absorbance detector at 280 nm) has been obtained over the concentration range of 0.5 to 40 microM. The detection limit for alpha-, beta- and kappa-caseins ranged between 0.35 and 0.70 microM. The precision of the method was evaluated, the coefficient of variation for alpha-, beta- and kappa-casein determination ranging between 3.0 and 6.0%. The method has been validated by the analysis of reference skim milk powder (BCR-063R) certificated for total nitrogen content. The method was applied to commercial casein mixture and to the qualitative and quantitative analysis of casein fractions in unprocessed, raw cows', goats' and ewes' milk (10 samples analyzed for each species), in one sample of unprocessed buffalos' milk and in commercial cheeses (mozzarella, robiola, ricotta and stracchino). Binary mixtures of milk (cow/goat and cow/ewe) were also analyzed and the ratio between casein peak areas (alpha(s1)/kappa, alpha(s2)/beta, beta/kappa and alpha(s2)/alpha(s1)) of the HIC chromatograms was proposed and discussed in order to evaluate a possible application of this method to detect milk adulteration.

Animals↗
PubMed1978

Stabilization of casein mRNA by prolactin and glucocorticoids.

Prolactin injected into pseudopregnant rabbits led to a parallel enhancement of casein synthesis and casein mRNA concentration. When this stimulation was followed by a withdrawal of prolactin obtained by injections of bromocriptine, the rate of casein synthesis progressively diminished. In the presence of endogenous prolactin after the initial stimulation, the decline of casein synthesis was delayed. Hydrocortisone acetate injected with bromocriptine after the initial stimulation by prolactin was able to maintain a high rate of casein synthesis. Measurements of casein mRNA concentration by hybridization with casein cDNA indicated that in all cases the amount of casein mRNA was correlated with the magnitude of casein synthesis. This suggests that the lactogenic hormones, prolactin and glucocorticoids, which were previously demonstrated to be responsible for the enhancement of casein mRNA concentration are involved in their stabilization.

Animals↗
PubMed1979

Role of glucocorticoids and progesterone in the development of rough endoplasmic reticulum involved in casein biosynthesis.

Hydrocortisone acetate injected into pseudopregnant rabbits induced casein synthesis and a parallel accumulation of casein mRNA. These effects were not accompanied by any enrichment of total RNA in the mammary cell. Hydrocortisone acetate did not favour the attachment of polysomes to endoplasmic reticulum. Casein mRNA concentration was enhanced in free and membrane-bound polysomes. After long treatments, the concentration of casein mRNA reached a plateau in membrane bound polysomes whereas it continued to be accumulated in free polysomes, suggesting that a substantial part of casein synthesis is then carried out by free polysomes. Progesterone injected with high doses of prolactin was unable to prevent the stimulatory action of prolactin on the synthesis of casein, the accumulation of casein mRNA and mammary gland growth, as judged by DNA content. By contrast, the increase in the total RNA content of mammary gland was still significantly reduced by progesterone. In addition, progesterone inhibited almost completely the formation of membrane-bound polysomes and the anchorage of casein mRNA to endoplasmic reticulum. From these data, it was concluded that the formation of the endoplasmic reticulum is not a prerequisite for the initiation of casein synthesis. Glucocorticoids do not play a major role in the formation of the endoplasmic reticulum and the Golai apparatus and in the binding of casein synthesizing polysomes to membranes. Progesteronne is capable of inhibiting preferentially and gradually the stimulation of cellular functions requiring the most potent prolactin stimulation.

Animals↗