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Protein of rabbits

Myofibrillar Structural Proteins of Rabbit Skeletal Muscle ... [Pg.547]

Herbivores that commonly feed on tannin-rich plants have evolved interesting methods to lessen the effect of ingested tannins on their digestive systems. For example, the salivary proteins of rabbits and other rodents are high in the amino acid proline, which has a very high affinity for tannins. Eating food high in tannins stimulates the secretion of these proteins and diminishes the toxic effect of the tannins. [Pg.98]

E. Casali, P. H. Petra, and J. B. A. Ross, Fluorescence investigation of the sex steroid binding protein of rabbit semm Steroid and subunit dissociation, Biochemistry 29, 9334-9343 (1990). [Pg.56]

Several observations indicate the formation of starch-protein complexes. For instance, starch precipitates serum proteins of rabbit, horse, sheep, and chicken.962 This observation seemingly indicates that the complexation has a rather universal character. On the other hand, the type of bonding of proteins from Triticum durum and Triticum sativum is specific for each of these varieties.963 The observed effects may not be associated with complex formation, but they can instead be attributed to the destruction of micelles by dehydration, followed by agglomeration.964 As in the case of starch complexes with sugars, the effect of proteins and cellulose derivatives on starch gelation can be assumed to be the result of the competition for water in solution. As a consequence, swelling is perturbed.965-968... [Pg.405]

White, D.A. (1977) The Biosynthesis of Mannose-Containing Lipids as Intermediates in the Glycosylation of Proteins of Rabbit Mammary Gland , Biochemical Society Transactions,... [Pg.339]

Borsook, H., Deasy, C. L., Haagen-Smit, A. J., Keighley, G., and Lowy, P. H., 1952, Incorporation in vitro of labeled amino acids into protein of rabbit reticulocytes, J. Biol. Chem. 196 669. [Pg.283]

Table VI contains an example of results obtained when the proteins of rabbit reticulocytes, after the incorporation of labeled amino acids, were submitted to a variety of treatments. All the results are in accord with the interpretation that the labeled amino acids were incorporated by... Table VI contains an example of results obtained when the proteins of rabbit reticulocytes, after the incorporation of labeled amino acids, were submitted to a variety of treatments. All the results are in accord with the interpretation that the labeled amino acids were incorporated by...
Table IX contains an example of results obtained when the proteins of rabbit reticulocytes, after the incorporation of labeled amino acids, were submitted to a variety of treatments. All the results are in accord with the interpretation that the labeled amino acids were incorporated by peptide bonds. Practically none of the incorporated amino acids (histidine was not determined because of methodical difficulties) were in an end (NHj) group position. This is in accord with the finding of Porter and Sanger (94), who determined the end (NH2) groups in the... Table IX contains an example of results obtained when the proteins of rabbit reticulocytes, after the incorporation of labeled amino acids, were submitted to a variety of treatments. All the results are in accord with the interpretation that the labeled amino acids were incorporated by peptide bonds. Practically none of the incorporated amino acids (histidine was not determined because of methodical difficulties) were in an end (NHj) group position. This is in accord with the finding of Porter and Sanger (94), who determined the end (NH2) groups in the...
The mature red blood cell cannot synthesize protein. Reticulocytes are active in protein synthesis. Once reticulocytes enter the circulation, they lose their intracellular organelles (ribosomes, mitochondria, etc) within about 24 hours, becoming young red blood cells and concomitandy losing their ability to synthesize protein. Extracts of rabbit reticulocytes (obtained by injecting rabbits with a chemical—phenylhydrazine—that causes a severe hemolytic anemia, so that the red cells are almost completely replaced by reticulocytes) are widely used as an in vitro system for synthesizing proteins. Endogenous mRNAs present in these reticulocytes are destroyed by use of a nuclease, whose activity can be inhibited by addition of Ca +. The system is then pro-... [Pg.611]

VHL Lee, DJ Schanzlin, RE Smith. (1986). Interaction of rabbit conjunctival mucin with tear protein and peptide analogs. In FJ Holly, ed. The Preocular Tear Film in Health, Disease, and Contact Lens Wear. Lubbock, TX Dry Eye Institute, pp 341-355. [Pg.378]

The plant is known to contain chelerythrine chloride, which inhibits the aggregation of rabbit platelet in vitro via inhibition on thromboxane formation and phosphoinosi-tides breakdown (30). Chelerythrine, which occurs in members of the family Papaver-aceae, has been reported to inhibit the enzymatic activity of protein kinase C and to exert cell-growth inhibitory effect via the induction of apoptosis in numerous cancer cell lines (31,32). What is the topoisomerase activity of chelerythrine ... [Pg.191]

Louis, C.F., Saunders, M.J., and Holroyd, J.A. (1977) The cross-linking of rabbit skeletal muscle sarcoplasmic reticulum protein. Biochim. Biophys. Acta 493, 78-92. [Pg.1090]

Dog gastric lipase CaMV enhanced 35S promoter/ CaMV 35S terminator LP of rabbit gastric lipase precursor LP of sweet potato sporamin precursor N. tabacum (leaves secretion) N. tabacum (leaves vacuole) 7% of acid extractable proteins 5% of acid extractable proteins 51... [Pg.97]

Use unconjugated protein A (36 pg/mL in SC) to block protein A binding sites on the Fc portion of rabbit anti-sheep. [Pg.301]

Table II. Percentage Distribution of Lipoproteins fed Various Proteins from Rabbits... Table II. Percentage Distribution of Lipoproteins fed Various Proteins from Rabbits...
A protein of similar molecular weight to that of rat oncomodulin, rat and rabbit parvalbumins, S100, and the vitamin D-dependent calcium-binding proteins has been isolated from chicken gizzard smooth muscle. In this case, however, the fluorescence emission from the four tyrosine residues is quenched by Ca2+ binding.(160) The decrease in fluorescence intensity was used to suggest that there are two different classes of Ca2+binding sites. [Pg.36]

Jerdeva GV, Wu K, Yarber FA, Rhodes CJ, Kalman D, Schechter JE, and Hamm-Alvarez SF [2005] Actin and non-muscle myosin H facilitate apical exocytosis of tear proteins in rabbit lacrimal acinar epithelial cells. J Cell Sci 118 4797-4812... [Pg.366]


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See also in sourсe #XX -- [ Pg.154 , Pg.155 ]




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