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6 results on '"G M, Nagel"'

1. Abstracts of papers Rational use of drugs

Author

M. N. G. Dukes, Robert M. Elenbaas, G. Tognoni, Dorothy L. Smith, Inga Lunde, H. G. M. Leufkens, Y. A. Hekster, A. Bakker, G. Ostino, H. Petri, F. Sturmans, H. D. Banta, F. F. H. Rutten, L. L. Martens, P. R. Noyce, F. W. H. M. Merkus, Lolkje de Jong-v.d.Berg, Flora Haaijer-Ruskamp, Graham Dukes, B. -M. Vidgren, S. Vidgren, N. Martini, M. L. Sala, G. Scroccaro, P. Olivencia, D. C. McLcod, W. G. Coln, A. G. Hartzcma, C. F. Thaver, J. M. Rodriguez-Sasiain, B. Sangroniz, M. D. Mauleon, M. A. Wood, M. J. Martinez, O. Leinebø, J. N. Saugen, P. Marini, R. Olivato, C. Alberola, E. Cruz-Martos, T. Cruz, N. Marfagon, A. Herreros de Tejada, P. Denig, F. M. Haaijer-Ruskamp, H. Wesseling, A. Versluis, M. P. Gascón, Robert Horne, Jane Hough, N. S. Klazinga, J. J. -E. van Everdingen, P. J. van den Broek, D. K. Roberts, G. B. A. Veitch, K. K. C. Tan, D. A. Holland, M. C. Allwood, A. Nicholls, A. Astobieta, R. Calvo, J. M. Rodriquez-Sasiain, D. Barriquand, C. Pochon, G. Aulagner, A. Vial, C. Dumarest, P. H. Maire, R. W. Jelliffe, J. R. B. J. Brouwers, K. Cramer, J. Gulyas, H. J. vd Kam, J. Sijtsma, C. Donadio, G. Tramonti, G. Garcea, M. Costagli, A. Lucchetti, R. Giordani, G. Paizis, R. Pierotti, G. Falcone, C. Bianchi, C. Gallastegui, R. Farré, I. Jiménez, M. A. Mangues, E. Guasch, G. Ginovart, X. Sagrera, F. Raspall, J. M. Queralto, J. M. Kovarik, C. M. A. Rademaker, J. Verhoef, L. Silvestri, M. Caputo, M. Andrew, E. -L. Toverud, I. Jimenez, I. Castro, E. Alvarez, J. Altimiras, J. J. J. P. M. van de Leur, N. F. Muller, J. M. Van Turnhout, L. Mendizabal, J. M. Rodriguez Sasiain, G. Morana, K. Moss Ofstad, A. -M. Timenes, J. K. F. Vroom, L. T. W. de Jong-van den Berg, P. B. van den Berg, J. J. de Gier, J. Ferres, O. Recoder, Rio T. Sanchez, M. P. Garcia, A. Julia, A. Balet, R. Farre, M. A. Manques, T. Berod, E. Dufay, C. Naveau, M. Combe, A. Sauvageon, Erik Wind Hansen, Jens Dencker Christensen, L. Lie-A-Huen, J. H. Kinqma, D. K. P. Meijer, F. Le Meur, P. Isoard, M. S. Salek, A. Y. Finlay, G. K. Khan, D. K. Luscombe, A. Stuurman, M. P. Boidin, K. Wallenius, R. Ojala, A. Kariluoto, M. Ikonen, A. H. P. Paes, A. Th. G. Blom, S. Wallenius, H. Enlund, K. Vainio, C. Codina, M. Roca, P. Sardà, N. Corominas, J. Massó, J. Ribas, K. Kentra, M. Myllyntausta, M. Saarenpää, M. S. A. Airaksinen, L. Mendarte, A. Rimola, R. Meisters, Y. Hekster, W. Janssen, A. Cox, R. Kempen, S. J. A. Aerdts, R. van Dalen, H. A. L. Clasener, J. Festen, PP Schjphorst, HB Benraad, P. van Asten, R. de Wit, R. J. G. Limbeek, H. G. M. Nagel, R. H. B. Mgyboom, B. H. C. Stricker, B. A. M. van den Berg, T. H. A. Nelen, T. A. G. Tijssen, P. Wassink, M. J. E. Wassink-L'Ortije, P. Gascón, C. Selva, T. Bassons, C. Pardo, M. P. Mas, M. Saqalés, F. Sánchez, V. Mercade, R. Pujol, C. Agustí, M. Cano, T. Gurrera, M. Gorchs, X. Fabregas, L. L. Murgui, A. Verdaguer, W. P. J. Witjes, E. J. Vollaard, B. J. P. Crul, C. Limpens, K. Ahonen, T. Klaukka, I. Vohlonen, J. Martikainen, Daniel Goldenberg, Andres Brodsky, Ines Aparici, Cecilia Argeri, D. Goldenberg, C. Saidman, L. Sevinski, N. Allevato, B. Mujico, J. Ubogui, P. Dorfman, Lupo L. Rodriguez, M. Varela, J. Higa, Annie Fourrier, Philippe Larrouturou, Claire Samarran, Jacqueline Huchet, N. D. Barber, N. Party, P. Wilson, Grethe Eide, Kari Horvei, Angelika Kruse-Jensen, Ingrid Wold, Turid Møark, C. W. Barrett, A. C. Tugwell, B. Søndergaard, M. Rasmussen, F. Davidsen, H. Hey, L. Kierkeby, L. Riis, M. Korhonen, P. Vidgren, T. Ojanen, M. Vidqren, J. Ferrés, T. Sanchez, C. Gallastequi, A. Julià, R. M. C. Herings, B. H. Ch. Stricker, A. J. H. H. Janssen, Heike Dinter, A. J. H. M. Janssen, X. Barbaut, S. Proust, G. Amlagner, F. A. L. M. Eskens, E. Arnoldussen, E. Sieradzki, E. Wanat-Słupska, M. Zlółkowska, I. Pankowska, R. Mazur, B. Ksiazkiewicz, A. Jankowski, A. Marzec, C. Marzec, M. O. Marzec, J. P. Marzec, D. R. Mungall, Lynne Portnoy, F. Lucas, F. Kadir, A. Pijpers, A. Vulto, J. Zuidema, P. Sutton, Antal Samu, John E. Murphy, Ronnie Chapman, Nicolien Wieringa, J. Rolloos, M. T. P. J. Voesten, P. J. J. de Meijer, G. H. P. de Koning, S. Salek, E. Reerink, L. Farrow, G. Raskob, D. Rosenbloom, R. Hull, A. Torras, O. Recorder, C. Torras, J. Cubellsl, M. Font, R. Madridejos, A. Catalán, M. Huguet, N. Franquesa, J. Gratacós, M. Martinez, A. Saltó, E. van der Kleijn, R. J. M. ter Wee, N. Holmberg, and R. F. Brenninkmeijer

Subjects
Pharmacology, Medical education, business.industry, Pharmacology (medical), Pharmacy, business, Psychology, Rational use
Published
1989

2. The size and shape of heart and muscle ferritins analyzed by sedimentation, gel filtration, and electrophoresis

Author

Maria C. Linder, D M Hungerford, M. Roboz, and G. M. Nagel

Subjects
Chromatography, Molecular mass, biology, Protein subunit, Size-exclusion chromatography, Skeletal muscle, Spleen, Cell Biology, Biochemistry, Ferritin, Electrophoresis, medicine.anatomical_structure, Sedimentation equilibrium, medicine, biology.protein, Molecular Biology
Abstract

We have compared the size and shape of ferritins from human heart, rat heart, and skeletal muscle with those of rat liver and horse spleen ferritins, using sedimentation and gel filtration techniques. The electrophoretically "fast" form of heart ferritin was partially separated from both the "slow" heart form and from rat liver ferritin by gel filtration (Stokes radii 72 A versus 69 and 68.5 A). Sedimentation velocity after iron removal showed an 18.5 S boundary even for mixtures of the two heart species, versus 17.3 S for rat liver and horse spleen apoferritins. Holoferritins gave a broad boundary, with coefficients from 66-80 S depending on iron content. Variable amounts of disaggregated ferritin (2.6 S) were also present in the heart ferritin preparations. Removal of iron significantly increased the electrophoretic migration of the fast but not the slow heart ferritin species. By sedimentation equilibrium, the molecular weights of all apoferritins save the fast heart form were about 490,000; that for the latter was near 750,000. Since electrophoresis revealed no major differences in subunit size, it is concluded that the larger, more asymmetric form of muscle ferritin contains 34 to 38 rather than 24 subunits.

Published
1981

3. The size and shape of heart and muscle ferritins analyzed by sedimentation, gel filtration, and electrophoresis

Author

M C, Linder, G M, Nagel, M, Roboz, and D M, Hungerford

Subjects
Protein Conformation, Muscles, Myocardium, Diaphragm, Rats, Molecular Weight, Liver, Species Specificity, Organ Specificity, Ferritins, Animals, Humans, Female, Horses, Spleen
Abstract

We have compared the size and shape of ferritins from human heart, rat heart, and skeletal muscle with those of rat liver and horse spleen ferritins, using sedimentation and gel filtration techniques. The electrophoretically "fast" form of heart ferritin was partially separated from both the "slow" heart form and from rat liver ferritin by gel filtration (Stokes radii 72 A versus 69 and 68.5 A). Sedimentation velocity after iron removal showed an 18.5 S boundary even for mixtures of the two heart species, versus 17.3 S for rat liver and horse spleen apoferritins. Holoferritins gave a broad boundary, with coefficients from 66-80 S depending on iron content. Variable amounts of disaggregated ferritin (2.6 S) were also present in the heart ferritin preparations. Removal of iron significantly increased the electrophoretic migration of the fast but not the slow heart ferritin species. By sedimentation equilibrium, the molecular weights of all apoferritins save the fast heart form were about 490,000; that for the latter was near 750,000. Since electrophoresis revealed no major differences in subunit size, it is concluded that the larger, more asymmetric form of muscle ferritin contains 34 to 38 rather than 24 subunits.

Published
1981

4. Resolution and characterization of a major protein of the sea urchin hyaline layer

Author

J, Gray, R, Justice, G M, Nagel, and E J, Carroll

Subjects
Chromatography, Hyalin, Chemical Phenomena, Light, Chemistry, Physical, Magnesium Chloride, Proteins, Molecular Weight, Calcium Chloride, Sea Urchins, Animals, Chemical Precipitation, Scattering, Radiation, Female, Magnesium, Gels, Ultracentrifugation, Ovum
Abstract

A major protein component of the gel-like, embryonic hyaline layer of Strongylocentrotus purpuratus has been purified and characterized. The protein retains the ability to form an insoluble gel in the presence of specific divalent cations, a property characteristic of the hyaline material. Using a light scattering assay developed to measure the initial rate of hyalin gelation, we have been able to show that calcium alone is capable of initiating this reaction but that calcium and magnesium are synergistic in their effect. In the absence of divalent cations, the major hyalin protein has a molecular weight of 9.2 +/- 0.5 X 10(5) and a sedimentation coefficient of 11.6 S; these and other data indicate that the protein assumes a very elongated, rod-like structure in solution. Smaller amounts of two additional proteins, 8.8 and 6.5 S, are present in the hyalin fraction when the jelly coat and vitelline layer are subjected to a more stringent acid treatment early in the isolation procedure.

Published
1986

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