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Guinea pig milk

A protein of Mr 55,000 in guinea pig milk lipid globule membranes appears to be similar but not identical to the bovine proteins using peptide mapping techniques and solubility in aqueous solutions as comparative criteria (Johnson et al. 1985). This protein is synthesized in a membrane-bound form and becomes progressively solubilized after incorporation into intracellular membranes (Mather et al 1984), a property shared by several other peripheral membrane proteins, e.g., the glycoprotein GP2 in the pancreas (Scheffer et aL 1980). [Pg.549]

Johnson, V. G., and Mather, I. H. 1985. Monoclonal antibodies prepared against PAS-I, butyrophilin and GP-55 from guinea-pig milk-fat-globule membrane bind specifically to the apical pole of secretory-epithelial cells in lactating mammary tissue. Exp. Cell Res. 156, 144-158. [Pg.573]

Guinea pigs milk contains a high level of LPL (20-50-fold that of cows milk), with more than 90% in the skim (Hamosh and Scow, 1971). Guinea pig LPL has been purified and found to be very similar in molecular structure and properties to the LPLs of cows and human milks (Wallinder et al., 1982 Bengtsson-Olivecrona et al., 1986). [Pg.488]

LPL activity in rats milk is only about 0.2% of that of guinea pigs milk, probably reflecting interspecial differences in milk secretory processes (Hamosh and Scow, 1971). Activity in dogs and cats milk is also low, of a similar order to human milk (Freed et al., 1986). [Pg.488]

Wallinder, L., Bengtsson, G., Olivecrona, T. 1982. Purification and properties of lipoprotein lipase in guinea pig milk. Biochim. Biophys. Acta 711, 107-113. [Pg.555]

The highest concentration of xanthine oxidase in mammals is found in the milk and lactating mammary gland [78, 92], although it is not known whether all species secrete the enzyme in milk. For obvious reasons, nearly all the information available refers to xanthine oxidase from bovine milk, but in fact both rat and guinea-pig milk have a higher enzyme content [92]. Table 3.2... [Pg.94]

Panoutsopoulos GI, Beedham C. Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes. Acta Biochim Pol 2004 51(3) 649-663. [Pg.105]

Selected entries from Methods in Enzymology [vol, page(s)] Detergent-resistant phospholipase Ai from Escherichia coll membranes, 197, 309 phospholipase Ai activity of guinea pig pancreatic lipase, 197, 316 purification of rat kidney lysosomal phospholipase Ai, 197, 325 purification and substrate specificity of rat hepatic lipase, 197, 331 human postheparin plasma lipoprotein lipase and hepatic triglyceride lipase, 197, 339 phospholipase activity of milk lipoprotein lipase, 197, 345. [Pg.554]

Ecobichon DJ, Hidvegi S, Comeau AM, et al. 1983. Transplacental and milk transfer of polybrominated biphenyls to perinatal guinea pigs from treated dams. Toxicology 28 51-63. [Pg.420]

Lactoferrm, found tn mother s milk, appears to be the most potent antibacterial transferrin and seems to play a role in the protection of breast-fed infants from certain infectious diseases. It has been claimed that milk proteins remain intact in the infant s stomach for up to 90 minutes and then pass into the small intestine unchanged, thus retaining their iron-binding capacity. In guinea pigs, addition of hematin to the diet abolishes the protective effects of the mother s milk. 09... [Pg.1004]

Mather, I. H., Bruder, G., Jarasch, E.-D., Heid, H. W. and Johnson, V. G. 1984. Protein synthesis in lactating guinea-pig mammary tissue perfused in vitro. II. Biogenesis of milk-fat-globule membrane proteins. Exp. Cell Res. 151, 277-282. [Pg.576]

Devey, M.E., Anderson, K.J., and Coombs, R.R.A. 1976. The modified anaphylaxis hypothesis for cot death. Anaphylactic sensitisation in guinea pigs fed cow s milk. Clin Exp Immunol 26 542-548. [Pg.124]

Lipase activity has been detected in the milk of many other species and, where characterized, is generally serum-stimulated (e.g., goat, buffalo, horse, guinea pig, rat, rabbit, cat, and dog) (Hamosh and Scow, 1971 Jensen and Pitas, 1976 Freed et al., 1986). With few exceptions, LPL appears to be the only significant indigenous lipase in milk. BSSL occurs in the milk of a small number of species (Section 2.2). [Pg.487]

Hamosh, M., Scow, R.O. 1971. Lipoprotein lipase activity in guinea pig and rat milk. Biochim. [Pg.541]

In the early 1960s Hassid and collaborators demonstrated that the enzyme lactose synthetase (now synthase) exists as a microsomal enzyme in the mammary glands of lactating cows and guinea pigs (Watkins and Hassid, 1962) and in a soluble form in cow milk (Babad and Hassid, 1964, 1966). They confirmed an earlier suggesdon by Wood and co-... [Pg.178]

Finally, there are temporal differences in the expression of milk proteins (e.g., casein and a-lactalbumin) among species, exemplified by the rat, guinea pig, and kangaroo (see, e.g., Hall and Campbell, 1986 Bur-ditt et al., 1981). The precise causes of these differences rem iin to be elucidated. [Pg.299]

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]


See other pages where Guinea pig milk is mentioned: [Pg.544]    [Pg.545]    [Pg.546]    [Pg.550]    [Pg.551]    [Pg.551]    [Pg.571]    [Pg.573]    [Pg.149]    [Pg.188]    [Pg.333]    [Pg.544]    [Pg.545]    [Pg.546]    [Pg.550]    [Pg.551]    [Pg.551]    [Pg.571]    [Pg.573]    [Pg.149]    [Pg.188]    [Pg.333]    [Pg.206]    [Pg.1562]    [Pg.277]    [Pg.1608]    [Pg.20]    [Pg.525]    [Pg.539]    [Pg.551]    [Pg.176]    [Pg.119]    [Pg.212]    [Pg.218]    [Pg.48]    [Pg.142]    [Pg.79]    [Pg.126]    [Pg.1004]    [Pg.336]    [Pg.171]   
See also in sourсe #XX -- [ Pg.21 ]




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