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Nucleo-proteins

Rabies virus glycoprotein (G)and nucleo-protein (N) Alfala mosaic virus and tobacco mosaic vims in tobacco and spinach leaf Elicited specific virus-neutralizing antibodies in mice. Immunogenic in mice when delivered orally and parenterally immunogenic in humans when delivered orally. Moderately protective against lethal challenge infection in mice. 16, 71... [Pg.137]

Weiss (W2) attributes the destruction of microorganisms to the OH and H radicals formed in the water near the nuclear material (Sec. IIIB2b). These radicals inactivate cells by initiating deamination and dephosphorylation of the nucleic acids, thus weakening the nucleo-protein structure. This and other proposed chemical mechanisms have recently been discussed by Gray (G12). [Pg.399]

This chapter provides a simplified overview of how researchers use the technique of X-ray crystallography to learn macromolecular structures. Chapters 3-8 are simply expansions of the material in this chapter. In order to keep the language simple, I will speak primarily of proteins, but the concepts I describe apply to all macromolecules and macromolecular assemblies that possess ordered structure, including carbohydrates, nucleic acids, and nucleo-protein complexes like ribosomes and whole viruses. [Pg.6]

Nucleo-proteins cyto-globulin, nucleo-histone. [Pg.398]

Pertmer, T. Robersts, T. Hynes, J. Influenza virus nucleo-protein-specific immunoglobulin G subclass and cytokine responses elicited by DNA vaccination are dependent on the route of vector DNA delivery. J. Virology 1996, 70, 6119-6125. [Pg.1361]

On the contrary, the desquamation processes appear to be less pronounced in the patients with a 15-30% skin surface involvement. In these patients the main effect of the increased cellular and nucleo-protein turnover is therefore able to induce an increase in both the serum urate levels and the total pool values (besides the expected increase in the total turnover rate), since the extrarenal loss due to direct skin desquamation is not so important as to counterbalance this primary metabolic effect. [Pg.283]

The ribosome has been a favorite nucleo-protein for study by neutron scattering (References in (3)). We shall mention briefly a recent experiment which made use of the scattering curve I(Q) and [H2O] [ D2O ] variation in the solvent (3). Electron micrographs of 16S RNA had been obtained and showed it to have a Y shaped structure. Is this structure maintained within the 30 S ribosome particle The scattering curve of the model was calculated and compared with neutron data. In 42% D2O, the excess scattering mass of protein is negligible, so that data collected from the 30 S in this buffer should only reflect the RNA structure within the particle. The... [Pg.301]

It should be recognized, however, that bacteriophages are not nucleo-proteins in the ordinary sense (1) they have complex morphological structure just below the microscopically resolvable range (2) the lethal and reproductive activities have been separated and ascribed to the protein membrane or ghost and to the nucleic acid, respectively ... [Pg.178]

Histidine is an essential amino acid in nutrition, and provides the iminazole ring necessary for synthesis of purines and nucleo-proteins. It forms neither glucose nor acetoacetic acid in the diabetic animal, though it is attacked by histidase, the enzyme present in vertebrate liver, which converts it into a compound that yields glutamate on alkaline hydrolysis. [Pg.313]

Transformation and Degradation of Purine in Animals.—Animals other than birds and reptiles excrete their waste protein nitrogen in the urine, and are said to be ureotelic. In ureotelic animals, purine metabolism proceeds along independent lines. The purines of the diet, chiefly nucleotides and nucleosides liberated from nucleo-proteins, are resolved into their constituent amino purines by the enzymes of the alimentary tract and mucosa. The amino purines are absorbed into the portal s3rstem, and if not utilised, are de-aminated by the appropriate enzjones, adenase and guanase, found in the liver. [Pg.350]

Bradshaw, L. J., Rosser, L. H., Jr. Inhibition of Ehrlich ascites tumor growth by nucleo-protein. I. In vivo characterization and presumptive chemical identification. J. nat. Cancer Inst. 43, 521—526 (1969). [Pg.97]

Suzuki, Ke., Watanabe, I. (2) Studies on nucleosalmine. II. Formation of artificial nucleo-proteins and the influence by pH (in Japanese). Nippon Kagaku Zasshi (J. Chem. Soc. Japan, Pure Chem. Sect.) 73, 825—827 (1952). [Pg.107]

Nucleosome Smallest repeat unit of chromatin nucleo-protein, containing 145 bp of DNA wrapped around a histone octamer core (2 subunits each of histone H2A, H2B, H3, and H4) along with linker DNA of variable length. Mild treatment of chromatin with DNase digests the linker and generates nucleosome fragments of different repeat lengths ( ladder ). [Pg.116]

Fig. 10. P-NMR spectra of DNA and nucleo-protein complexes, (a) Solid fibrous calf thymus DNA. (b) Chicken erythrocyte chromatin in solution. (c) Bull sperm heads in solution, (d) High-molecular-weight calf thumus DNA in solution. Spectra (a), (b), and (c) resulted from cross-polarization with 1-ms mix time and 1-s recycle delay. Data were acquired for 10 ms with a 2.3-mT H decoupling field. Spectrum (d) was from n/2 pulses rather than cross-polarization. From EMVeidi el al. (1981). Fig. 10. P-NMR spectra of DNA and nucleo-protein complexes, (a) Solid fibrous calf thymus DNA. (b) Chicken erythrocyte chromatin in solution. (c) Bull sperm heads in solution, (d) High-molecular-weight calf thumus DNA in solution. Spectra (a), (b), and (c) resulted from cross-polarization with 1-ms mix time and 1-s recycle delay. Data were acquired for 10 ms with a 2.3-mT H decoupling field. Spectrum (d) was from n/2 pulses rather than cross-polarization. From EMVeidi el al. (1981).

See other pages where Nucleo-proteins is mentioned: [Pg.333]    [Pg.440]    [Pg.49]    [Pg.1497]    [Pg.141]    [Pg.9]    [Pg.92]    [Pg.201]    [Pg.975]    [Pg.43]    [Pg.513]    [Pg.513]    [Pg.515]    [Pg.515]    [Pg.516]    [Pg.517]    [Pg.521]    [Pg.521]    [Pg.551]    [Pg.429]    [Pg.90]    [Pg.406]    [Pg.224]    [Pg.349]    [Pg.2488]    [Pg.177]    [Pg.187]    [Pg.130]    [Pg.348]    [Pg.210]   
See also in sourсe #XX -- [ Pg.398 ]




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Bibliography on Enzymes of the Nucleo-proteins

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