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Casein rabbits

Figure 4 Reduction of immunoreactivity upon digestion of casein with different proteases. Competitive ELiSA was performed by using poiycionai anti-casein rabbit antibodies on sodium caseinate before (dots) and after controiied digestion with a protease of pancreatic (triangies) or bacteriai origin (squares). Figure 4 Reduction of immunoreactivity upon digestion of casein with different proteases. Competitive ELiSA was performed by using poiycionai anti-casein rabbit antibodies on sodium caseinate before (dots) and after controiied digestion with a protease of pancreatic (triangies) or bacteriai origin (squares).
Arsenic uptake in rabbit intestine is inhibited by phosphate, casein, and various metal-chelating agents (USEPA 1980). Mice and rabbits are significantly protected against sodium arsenite intoxication by (V-(2,3-dimercaptopropyl)phthalamidic acid (Stine et al. 1984). Conversely, the toxic effects of arsenite are potentiated by excess dithiols, cadmium, and lead, as evidenced by reduced food efficiency and disrupted blood chemistry in rodents (Pershagen and Vahter 1979). [Pg.1485]

Table I. Serum Lipids and Aortic Atherosclerosis in Rabbits fed Casein, Soy Protein, Casein Arginine, or Soy Lysine... Table I. Serum Lipids and Aortic Atherosclerosis in Rabbits fed Casein, Soy Protein, Casein Arginine, or Soy Lysine...
In addition to more rapid absorption of lipids in animals fed casein, another mechanism that may be operative is decreased clearance of circulating lipids. Rabbits fed a casein-based semipurified diet excreted significantly less cholesterol but more bile acids in their feces than animals fed a commercial diet (18). The total sterol excretion in feces of the animals fed the casein diet was half that of the rabbits fed the stock diet. Huff and Carroll (19) found that rabbits fed soy protein had a much faster turnover rate of cholesterol and a significantly reduced rapidly exchangeable cholesterol pool compared with rabbits fed casein. Similar studies performed in our laboratory revealed that the mean transit time for cholesterol was 18.4 days in rabbits fed soy protein, 36.8 days in rabbits fed casein, 33.7 days in rabbits fed soy plus lysine, and 36.3 days in rabbits fed casein plus arginine. These data suggest that addition of lysine to soy protein... [Pg.161]

Assays utilized conventional ELISA processing except that the reagent volumes were greatly reduced, ranging from 25- to 50-pL well additions. Following a 1-hr block in casein, the monoclonal detection antibody was incubated an additional hour at room temperature. The assay sensihvity from the micro-ELISA was approximately 13.4 ng/mL for rabbit IgG — a result similar to that reported by Silzel et al. (1998). The benefit of the "array of arrays" approach is that 96 samples could be processed for multiple (36 to 144) analytes within the same time interval as a standard single-analyte ELISA. [Pg.196]

Kuyvenhoven, M.W., Roszkowski, W.F., West, C.E., Hoogenboom, R.L., Vos, R.M., Beynen, A.C., and van der Meer, R. 1989. Digestibility of casein, formaldehyde-treated casein and soya-bean protein in relation to their effects on serum cholesterol in rabbits. Br. J. Nutr. 62, 331-342. [Pg.199]

ELISA of sheep IgM (antigen) was conducted in a PDMS chip. The capture antibody (rabbit anti-sheep IgM-HRP) was added. Then the fluorogenic substrate (HPPA) was added for fluorescent detection. The conventional blocking reagents (0.5% w/v BSA, 0.5% w/v casein, 0.5% v/v Tween-20), which normally worked for the polystyrene ELISA plate, did not work with the hydrophobic PDMS surface. To solve this problem, 4% PEG and 7% normal rabbit serum were included in the above solution for effective blocking [173]. [Pg.348]

Fig. 7. Consensus sequences of the signal peptides of (a) the three Ca2+-sensitive caseins and (b) the K-caseins, taken from sequences for the cow, sheep, man, guinea pig, rat, mouse, and rabbit. Fig. 7. Consensus sequences of the signal peptides of (a) the three Ca2+-sensitive caseins and (b) the K-caseins, taken from sequences for the cow, sheep, man, guinea pig, rat, mouse, and rabbit.
Otani, H. and Hata, I. 1995. Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer s patch cells by bovine milk caseins and their digests. J. Dairy Res. 62, 339-348. [Pg.265]

Polyclonal antibodies have been prepared against partially purified rabbit mammary gland receptors [42-44], and have been used to demonstrate that the receptors really are involved in mediating the biological actions of prolactin. Anti-receptor antibodies that blocked binding of labelled prolactin were able to inhibit prolactin-stimulated casein synthesis and amino acid transport in rabbit mammary gland explants in vitro [43,45] (Fig. 4). They had no effect on the actions of insulin... [Pg.301]

Fig. 4. Antibodies to the prolactin receptor block the actions of the hormone on casein synthesis in rabbit mammary tissue explants. CS, control serum AS, antiserum to receptor P, prolactin. Data from Ref. 45. Fig. 4. Antibodies to the prolactin receptor block the actions of the hormone on casein synthesis in rabbit mammary tissue explants. CS, control serum AS, antiserum to receptor P, prolactin. Data from Ref. 45.
More recently, monoclonal antibodies to the rabbit prolactin receptor have been described [49,50]. These showed strong species specificity, competed with 125I-la-belled prolactin for binding to receptors, and provided evidence for receptor heterogeneity in some tissues [49], Two of the monoclonal antibodies could block the actions of prolactin on casein synthesis in rabbit mammary gland explants, and one of them could inhibit milk production in vivo [50]. A third antibody could mimic the actions of prolactin on both casein and DNA synthesis in mammary explants. For this effect bivalency was essential, and down-regulation of receptors was much less than that produced by prolactin itself [50],... [Pg.302]

Bergeron, N., and Jacques, H. 1989. Influence of fish protein as compared to casein and soy protein on serum and hver hpids, and serum lipoprotein cholesterol levels in the rabbit. Atherosclerosis, 78,113-121. [Pg.513]

Chao, Y.S., Kroon, P.A., Yamin, T.T., Thompson, G.M., and Alberts, A.W. (1983). Regulation of hepatic receptor-dependent degradation of LDL by mevinolin in rabbits with hypercholesterolemia induced by a wheat starch-casein diet. Biochem Biophys Acta 754 134-141. [Pg.294]

The wisdom of requiring the employees to drink milk has been severely questioned for this reason Milk contains primarily fats and casein. The fats are capable of dissohing a large amotmt of TXT. Therefore, should any of the explosive accidentally find its way into the milk, or should there be any in the stomach through swallowing dust in the factory, this will dissolve in the fats of the milk and will be absorbed by the blood. This action has been proved by Dr. Haythom, who has performed several experiments upon rabbits and guinea pigs with a solution of TXT in milk. [Pg.120]

Wash in PBS-Tween 20, add polyclonal rabbit anti-NA sera in PBS-casein, and incubate 1 h at room temperature. [Pg.371]


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