896 resultados para Arquitectos - España - s. 20-21
Resumo:
The ecology of the lower marine fungi, namely the thraustochytrides, in the Fladen Ground area (FLEX box) and other parts of the North Sea was studied during 5 cruises in 1975 and 1976. The number of fungi/liter and the number of species showed seasonal fluctuations in the surface water samples from all the stations. A high number was found in September 1976 and a lower number in March 1976. These numbers, however, revealed no seasonal fluctuations in the underlying sediments. In both the surface waters and the sediments, a consistingly low number of fungi was recorded for certain stations and a high number of fungi for others, the reason for this beeing unknown. The sediments revealed a very high number of fungi/liter. Observations on the distribution of various species are presented. Certain species occured more frequently at some stations than at others; certain species occured more in the water column, e.g. Ulkenia minuta, and still others in the sediments, e.g. Thraustochytrium multirudimentale.
Resumo:
We aspire to shape the Constantine’s personality in particular by analyzing his loving relationship, first with Minervina and then with Fausta, and not forgetting the bond with his mother Helena, hence the reference to uxor, mater and concubina in our title. We will analyze if these women exercised any influence on the composition of his production rules and, if so, to what extent they were able to determine the historical development of the following decades. From this point of view we must consider in general the emperor had to combine their political claims and government with these relationships, showing great skill in handling times and ways, always putting the first to the second.
Resumo:
The Revised Iowa Energy Conservation Plan: 1979-1980 is a blue print for the state's continued participation. The original Plan contained descriptions of more than 70 programs underway or conceived for state implementation with federal dollars. The Revised Plan contains only those programs to be funded in Federal dollars. The projects include five mandatory programs identified by DOE and several projects selected for funding by the Iowa Energy Policy Council (EPC), the policy making board which governs the state energy agency. The 18-member Council selected the conservation programs at its March 20-21, 1979 meeting. The Council retains the right to amend both the Plan and the budget at any time for the duration of the three-year program.
Resumo:
En fecha reciente se ha observado, en una finca de café cerca de Santiago de María, una plaga del cafeto que es, sin duda alguna, nueva para El Salvador. No se tiene aún conocimiento de que haya aparecido en otras regiones cafetaleras de la República y de acuerdo con los caracteres de una plaga del cafeto estudiada en Haití por Charles H. Arndt y Herbert L. Dozier, la que se ha observado en Santiago de María es similar a la plaga que se descubrió en Haití en 1931. Esta plaga del cafeto encontrada en Santiago de María es causada por un grillo. Para evitar confusiones con otra plaga del cafeto investigada en El Salvador por la Dr. Vera Wellborn y denominada "El Grillo del Café" (Resolución del problema de la enfermedad, de la Antigua),también causada por otra clase de grillo, se ha optado por llamar la nueva plaga El Grillo Haitiano del Cafeto.
Resumo:
La invención comprende un sistema para la medición de campos electromagnéticos débiles, en la banda de frecuencias comprendida entre 1 a 100 Hz, donde se localizan señales derivadas de la resonancia natural que ocurre entre la tierra y la ionosfera, las resonancias de Schumann. El sistema está compuesto por un núcleo de material ferromagnético (1) y un conjunto de bobinas separadas entre s (2), conectadas mediante cables unifilares (8). Un cable de par trenzado (3) conecta el sensor a un sistema electrónico de medida (4) compuesto por un amplificador diferencial (5) al que se acoplan cada par trenzado, en una bifurcación coaxial con las mallas comunes (20), (21) mediante conectores coaxiales (22), (23) y con salida a un convertidor analógico digital (6). La geometría, estructura y materiales del sistema, le confieren sus propiedades de sensibilidad y ancho de banda.
Resumo:
A anchoita foi capturada e acondicionada a bordo sob-resfriamento a 0°C com gelo em escamas. Após o recebimento, o pescado foi processado na forma salgado-maturado. Após a maturação foram processadas e embaladas em sacos de polietileno e armazenadas sob-refrigeração a 5°C durante 84 dias. As amostras foram divididas grupos: (1) sob pressão atmosfera normal, (2) vácuo, (3) atmosfera modificada com 50% CO2 + 20% O2 + 30% N2 e (4) 60% CO2 + 10% O2 + 30% N2, em embalagens de polietileno e aluminizadas, termo-seladas e armazenadas sob-refrigeração a 5°C. Os valores de textura tiveram uma redução de 2277,8 N (Kg.m/s2 ) para 821,90 N (Kg.m/s2 ) para o tratamento controle. A qualidade inicial do pescado atendeu aos padrões legais vigentes, apresentando ausncia Salmonella sp e enumerações aceitáveis aos padrões de Staphylococcus coagulase positiva, Clostridium sulfito redutores, coliforme totais e a 45ºC. Com relação ao pH, houve diferenças significativas durante o tempo de processamento (p<0,05), o valor passou de 6,3 (início) para 6,4 (final). Com relação aos resultados correspondentes aos parâmetros L*, a* e b* (cor), em todos os tratamentos e ao longo do tempo de processamento (ambas as embalagens), ocorreram diferenças significativas (p<0,05). Os valores de L* variaram de 34,80 para 18,00 (controle) 23,00 (vácuo), 20,21 (T3) e 22,00 (T4) embalagens de polietileno. Nas embalagens de alumínio os valores de L* variaram de 34,00 para 25,00 (controle), 29,00(vácuo), 22,10 (T3) e 26,00 (T4).
Resumo:
Membrane proteins, which reside in the membranes of cells, play a critical role in many important biological processes including cellular signaling, immune response, and material and energy transduction. Because of their key role in maintaining the environment within cells and facilitating intercellular interactions, understanding the function of these proteins is of tremendous medical and biochemical significance. Indeed, the malfunction of membrane proteins has been linked to numerous diseases including diabetes, cirrhosis of the liver, cystic fibrosis, cancer, Alzheimer's disease, hypertension, epilepsy, cataracts, tubulopathy, leukodystrophy, Leigh syndrome, anemia, sensorineural deafness, and hypertrophic cardiomyopathy.1-3 However, the structure of many of these proteins and the changes in their structure that lead to disease-related malfunctions are not well understood. Additionally, at least 60% of the pharmaceuticals currently available are thought to target membrane proteins, despite the fact that their exact mode of operation is not known.4-6 Developing a detailed understanding of the function of a protein is achieved by coupling biochemical experiments with knowledge of the structure of the protein. Currently the most common method for obtaining three-dimensional structure information is X-ray crystallography. However, no a priori methods are currently available to predict crystallization conditions for a given protein.7-14 This limitation is currently overcome by screening a large number of possible combinations of precipitants, buffer, salt, and pH conditions to identify conditions that are conducive to crystal nucleation and growth.7,9,11,15-24 Unfortunately, these screening efforts are often limited by difficulties associated with quantity and purity of available protein samples. While the two most significant bottlenecks for protein structure determination in general are the (i) obtaining sufficient quantities of high quality protein samples and (ii) growing high quality protein crystals that are suitable for X-ray structure determination,7,20,21,23,25-47 membrane proteins present additional challenges. For crystallization it is necessary to extract the membrane proteins from the cellular membrane. However, this process often leads to denaturation. In fact, membrane proteins have proven to be so difficult to crystallize that of the more than 66,000 structures deposited in the Protein Data Bank,48 less than 1% are for membrane proteins, with even fewer present at high resolution (< 2Å)4,6,49 and only a handful are human membrane proteins.49 A variety of strategies including detergent solubilization50-53 and the use of artificial membrane-like environments have been developed to circumvent this challenge.43,53-55 In recent years, the use of a lipidic mesophase as a medium for crystallizing membrane proteins has been demonstrated to increase success for a wide range of membrane proteins, including human receptor proteins.54,56-62 This in meso method for membrane protein crystallization, however, is still by no means routine due to challenges related to sample preparation at sub-microliter volumes and to crystal harvesting and X-ray data collection. This dissertation presents various aspects of the development of a microfluidic platform to enable high throughput in meso membrane protein crystallization at a level beyond the capabilities of current technologies. Microfluidic platforms for protein crystallization and other lab-on-a-chip applications have been well demonstrated.9,63-66 These integrated chips provide fine control over transport phenomena and the ability to perform high throughput analyses via highly integrated fluid networks. However, the development of microfluidic platforms for in meso protein crystallization required the development of strategies to cope with extremely viscous and non-Newtonian fluids. A theoretical treatment of highly viscous fluids in microfluidic devices is presented in Chapter 3, followed by the application of these strategies for the development of a microfluidic mixer capable of preparing a mesophase sample for in meso crystallization at a scale of less than 20 nL in Chapter 4. This approach was validated with the successful on chip in meso crystallization of the membrane protein bacteriorhodopsin. In summary, this is the first report of a microfluidic platform capable of performing in meso crystallization on-chip, representing a 1000x reduction in the scale at which mesophase trials can be prepared. Once protein crystals have formed, they are typically harvested from the droplet they were grown in and mounted for crystallographic analysis. Despite the high throughput automation present in nearly all other aspects of protein structure determination, the harvesting and mounting of crystals is still largely a manual process. Furthermore, during mounting the fragile protein crystals can potentially be damaged, both from physical and environmental shock. To circumvent these challenges an X-ray transparent microfluidic device architecture was developed to couple the benefits of scale, integration, and precise fluid control with the ability to perform in situ X-ray analysis (Chapter 5). This approach was validated successfully by crystallization and subsequent on-chip analysis of the soluble proteins lysozyme, thaumatin, and ribonuclease A and will be extended to microfluidic platforms for in meso membrane protein crystallization. The ability to perform in situ X-ray analysis was shown to provide extremely high quality diffraction data, in part as a result of not being affected by damage due to physical handling of the crystals. As part of the work described in this thesis, a variety of data collection strategies for in situ data analysis were also tested, including merging of small slices of data from a large number of crystals grown on a single chip, to allow for diffraction analysis at biologically relevant temperatures. While such strategies have been applied previously,57,59,61,67 they are potentially challenging when applied via traditional methods due to the need to grow and then mount a large number of crystals with minimal crystal-to-crystal variability. The integrated nature of microfluidic platforms easily enables the generation of a large number of reproducible crystallization trials. This, coupled with in situ analysis capabilities has the potential of being able to acquire high resolution structural data of proteins at biologically relevant conditions for which only small crystals, or crystals which are adversely affected by standard cryocooling techniques, could be obtained (Chapters 5 and 6). While the main focus of protein crystallography is to obtain three-dimensional protein structures, the results of typical experiments provide only a static picture of the protein. The use of polychromatic or Laue X-ray diffraction methods enables the collection of time resolved structural information. These experiments are very sensitive to crystal quality, however, and often suffer from severe radiation damage due to the intense polychromatic X-ray beams. Here, as before, the ability to perform in situ X-ray analysis on many small protein crystals within a microfluidic crystallization platform has the potential to overcome these challenges. An automated method for collecting a "single-shot" of data from a large number of crystals was developed in collaboration with the BioCARS team at the Advanced Photon Source at Argonne National Laboratory (Chapter 6). The work described in this thesis shows that, even more so than for traditional structure determination efforts, the ability to grow and analyze a large number of high quality crystals is critical to enable time resolved structural studies of novel proteins. In addition to enabling X-ray crystallography experiments, the development of X-ray transparent microfluidic platforms also has tremendous potential to answer other scientific questions, such as unraveling the mechanism of in meso crystallization. For instance, the lipidic mesophases utilized during in meso membrane protein crystallization can be characterized by small angle X-ray diffraction analysis. Coupling in situ analysis with microfluidic platforms capable of preparing these difficult mesophase samples at very small volumes has tremendous potential to enable the high throughput analysis of these systems on a scale that is not reasonably achievable using conventional sample preparation strategies (Chapter 7). In collaboration with the LS-CAT team at the Advanced Photon Source, an experimental station for small angle X-ray analysis coupled with the high quality visualization capabilities needed to target specific microfluidic samples on a highly integrated chip is under development. Characterizing the phase behavior of these mesophase systems and the effects of various additives present in crystallization trials is key for developing an understanding of how in meso crystallization occurs. A long term goal of these studies is to enable the rational design of in meso crystallization experiments so as to avoid or limit the need for high throughput screening efforts. In summary, this thesis describes the development of microfluidic platforms for protein crystallization with in situ analysis capabilities. Coupling the ability to perform in situ analysis with the small scale, fine control, and the high throughput nature of microfluidic platforms has tremendous potential to enable a new generation of crystallographic studies and facilitate the structure determination of important biological targets. The development of platforms for in meso membrane protein crystallization is particularly significant because they enable the preparation of highly viscous mixtures at a previously unachievable scale. Work in these areas is ongoing and has tremendous potential to improve not only current the methods of protein crystallization and crystallography, but also to enhance our knowledge of the structure and function of proteins which could have a significant scientific and medical impact on society as a whole. The microfluidic technology described in this thesis has the potential to significantly advance our understanding of the structure and function of membrane proteins, thereby aiding the elucidation of human biology, the development of pharmaceuticals with fewer side effects for a wide range of diseases. References (1) Quick, M.; Javitch, J. A. P Natl Acad Sci USA 2007, 104, 3603. (2) Trubetskoy, V. S.; Burke, T. J. Am Lab 2005, 37, 19. (3) Pecina, P.; Houstkova, H.; Hansikova, H.; Zeman, J.; Houstek, J. Physiol Res 2004, 53, S213. (4) Arinaminpathy, Y.; Khurana, E.; Engelman, D. M.; Gerstein, M. B. Drug Discovery Today 2009, 14, 1130. (5) Overington, J. P.; Al-Lazikani, B.; Hopkins, A. L. Nat Rev Drug Discov 2006, 5, 993. (6) Dauter, Z.; Lamzin, V. S.; Wilson, K. S. Current Opinion in Structural Biology 1997, 7, 681. (7) Hansen, C.; Quake, S. R. Current Opinion in Structural Biology 2003, 13, 538. (8) Govada, L.; Carpenter, L.; da Fonseca, P. C. A.; Helliwell, J. R.; Rizkallah, P.; Flashman, E.; Chayen, N. E.; Redwood, C.; Squire, J. M. J Mol Biol 2008, 378, 387. (9) Hansen, C. L.; Skordalakes, E.; Berger, J. M.; Quake, S. R. P Natl Acad Sci USA 2002, 99, 16531. (10) Leng, J.; Salmon, J.-B. Lab Chip 2009, 9, 24. (11) Zheng, B.; Gerdts, C. J.; Ismagilov, R. F. Current Opinion in Structural Biology 2005, 15, 548. (12) Lorber, B.; Delucas, L. J.; Bishop, J. B. J Cryst Growth 1991, 110, 103. (13) Talreja, S.; Perry, S. L.; Guha, S.; Bhamidi, V.; Zukoski, C. F.; Kenis, P. J. A. The Journal of Physical Chemistry B 2010, 114, 4432. (14) Chayen, N. E. Current Opinion in Structural Biology 2004, 14, 577. (15) He, G. W.; Bhamidi, V.; Tan, R. B. H.; Kenis, P. J. A.; Zukoski, C. F. Cryst Growth Des 2006, 6, 1175. (16) Zheng, B.; Tice, J. D.; Roach, L. S.; Ismagilov, R. F. Angew Chem Int Edit 2004, 43, 2508. (17) Li, L.; Mustafi, D.; Fu, Q.; Tereshko, V.; Chen, D. L. L.; Tice, J. D.; Ismagilov, R. F. P Natl Acad Sci USA 2006, 103, 19243. (18) Song, H.; Chen, D. L.; Ismagilov, R. F. Angew Chem Int Edit 2006, 45, 7336. (19) van der Woerd, M.; Ferree, D.; Pusey, M. Journal of Structural Biology 2003, 142, 180. (20) Ng, J. D.; Gavira, J. A.; Garcia-Ruiz, J. M. Journal of Structural Biology 2003, 142, 218. (21) Talreja, S.; Kenis, P. J. A.; Zukoski, C. F. Langmuir 2007, 23, 4516. (22) Hansen, C. L.; Quake, S. R.; Berger, J. M. US, 2007. (23) Newman, J.; Fazio, V. J.; Lawson, B.; Peat, T. S. Cryst Growth Des 2010, 10, 2785. (24) Newman, J.; Xu, J.; Willis, M. C. Acta Crystallographica Section D 2007, 63, 826. (25) Collingsworth, P. D.; Bray, T. L.; Christopher, G. K. J Cryst Growth 2000, 219, 283. (26) Durbin, S. D.; Feher, G. Annu Rev Phys Chem 1996, 47, 171. (27) Talreja, S.; Kim, D. Y.; Mirarefi, A. Y.; Zukoski, C. F.; Kenis, P. J. A. J Appl Crystallogr 2005, 38, 988. (28) Yoshizaki, I.; Nakamura, H.; Sato, T.; Igarashi, N.; Komatsu, H.; Yoda, S. J Cryst Growth 2002, 237, 295. (29) Anderson, M. J.; Hansen, C. L.; Quake, S. R. P Natl Acad Sci USA 2006, 103, 16746. (30) Hansen, C. L.; Sommer, M. O. A.; Quake, S. R. P Natl Acad Sci USA 2004, 101, 14431. (31) Lounaci, M.; Rigolet, P.; Abraham, C.; Le Berre, M.; Chen, Y. Microelectron Eng 2007, 84, 1758. (32) Zheng, B.; Roach, L. S.; Ismagilov, R. F. J Am Chem Soc 2003, 125, 11170. (33) Zhou, X.; Lau, L.; Lam, W. W. L.; Au, S. W. N.; Zheng, B. Anal. Chem. 2007. (34) Cherezov, V.; Caffrey, M. J Appl Crystallogr 2003, 36, 1372. (35) Qutub, Y.; Reviakine, I.; Maxwell, C.; Navarro, J.; Landau, E. M.; Vekilov, P. G. J Mol Biol 2004, 343, 1243. (36) Rummel, G.; Hardmeyer, A.; Widmer, C.; Chiu, M. L.; Nollert, P.; Locher, K. P.; Pedruzzi, I.; Landau, E. M.; Rosenbusch, J. P. Journal of Structural Biology 1998, 121, 82. (37) Gavira, J. A.; Toh, D.; Lopez-Jaramillo, J.; Garcia-Ruiz, J. M.; Ng, J. D. Acta Crystallogr D 2002, 58, 1147. (38) Stevens, R. C. Current Opinion in Structural Biology 2000, 10, 558. (39) Baker, M. Nat Methods 2010, 7, 429. (40) McPherson, A. In Current Topics in Membranes, Volume 63; Volume 63 ed.; DeLucas, L., Ed.; Academic Press: 2009, p 5. (41) Gabrielsen, M.; Gardiner, A. T.; Fromme, P.; Cogdell, R. J. In Current Topics in Membranes, Volume 63; Volume 63 ed.; DeLucas, L., Ed.; Academic Press: 2009, p 127. (42) Page, R. In Methods in Molecular Biology: Structural Proteomics - High Throughput Methods; Kobe, B., Guss, M., Huber, T., Eds.; Humana Press: Totowa, NJ, 2008; Vol. 426, p 345. (43) Caffrey, M. Ann Rev Biophys 2009, 38, 29. (44) Doerr, A. Nat Methods 2006, 3, 244. (45) Brostromer, E.; Nan, J.; Li, L.-F.; Su, X.-D. Biochemical and Biophysical Research Communications 2009, 386, 634. (46) Li, G.; Chen, Q.; Li, J.; Hu, X.; Zhao, J. Anal Chem 2010, 82, 4362. (47) Jia, Y.; Liu, X.-Y. The Journal of Physical Chemistry B 2006, 110, 6949. (48) RCSB Protein Data Bank. http://www.rcsb.org/ (July 11, 2010). (49) Membrane Proteins of Known 3D Structure. http://blanco.biomol.uci.edu/Membrane_Proteins_xtal.html (July 11, 2010). (50) Michel, H. Trends Biochem Sci 1983, 8, 56. (51) Rosenbusch, J. P. Journal of Structural Biology 1990, 104, 134. (52) Garavito, R. M.; Picot, D. Methods 1990, 1, 57. (53) Kulkarni, C. V. 2010; Vol. 12, p 237. (54) Landau, E. M.; Rosenbusch, J. P. P Natl Acad Sci USA 1996, 93, 14532. (55) Pebay-Peyroula, E.; Rummel, G.; Rosenbusch, J. P.; Landau, E. M. Science 1997, 277, 1676. (56) Cherezov, V.; Liu, W.; Derrick, J. P.; Luan, B.; Aksimentiev, A.; Katritch, V.; Caffrey, M. Proteins: Structure, Function, and Bioinformatics 2008, 71, 24. (57) Cherezov, V.; Rosenbaum, D. M.; Hanson, M. A.; Rasmussen, S. G. F.; Thian, F. S.; Kobilka, T. S.; Choi, H. J.; Kuhn, P.; Weis, W. I.; Kobilka, B. K.; Stevens, R. C. Science 2007, 318, 1258. (58) Cherezov, V.; Yamashita, E.; Liu, W.; Zhalnina, M.; Cramer, W. A.; Caffrey, M. J Mol Biol 2006, 364, 716. (59) Jaakola, V. P.; Griffith, M. T.; Hanson, M. A.; Cherezov, V.; Chien, E. Y. T.; Lane, J. R.; IJzerman, A. P.; Stevens, R. C. Science 2008, 322, 1211. (60) Rosenbaum, D. M.; Cherezov, V.; Hanson, M. A.; Rasmussen, S. G. F.; Thian, F. S.; Kobilka, T. S.; Choi, H. J.; Yao, X. J.; Weis, W. I.; Stevens, R. C.; Kobilka, B. K. Science 2007, 318, 1266. (61) Wacker, D.; Fenalti, G.; Brown, M. A.; Katritch, V.; Abagyan, R.; Cherezov, V.; Stevens, R. C. J Am Chem Soc 2010, 132, 11443. (62) Höfer, N.; Aragão, D.; Caffrey, M. Biophys J 2010, 99, L23. (63) Li, L.; Ismagilov, R. F. Ann Rev Biophys 2010. (64) Pal, R.; Yang, M.; Lin, R.; Johnson, B. N.; Srivastava, N.; Razzacki, S. Z.; Chomistek, K. J.; Heldsinger, D. C.; Haque, R. M.; Ugaz, V. M.; Thwar, P. K.; Chen, Z.; Alfano, K.; Yim, M. B.; Krishnan, M.; Fuller, A. O.; Larson, R. G.; Burke, D. T.; Burns, M. A. Lab Chip 2005, 5, 1024. (65) Jayashree, R. S.; Gancs, L.; Choban, E. R.; Primak, A.; Natarajan, D.; Markoski, L. J.; Kenis, P. J. A. J Am Chem Soc 2005, 127, 16758. (66) Wootton, R. C. R.; deMello, A. J. Chem Commun 2004, 266. (67) McPherson, A. J Appl Crystallogr 2000, 33, 397.
Resumo:
La anticoncepción de emergencia se ha diseñado para evitar un embarazo no planificado. La sustancia usada para este fin es el levonorgestrel, que suprime el crecimiento folicular y el desarrollo del cuerpo lúteo. Lo que se ha pretendido con este estudio es determinar el nivel de conocimientos que tienen los estudiantes en cuanto a AE, sus actitudes y prácticas, respecto a esto. 300 alumnos de Medicina de la Universidad de Cuenca, fueron evaluados mediante formularios, todos ellos se encontraban en edades comprendidas entre 20-21 años. Se concluyó que la mayoría de estos, corresponden al sexo femenino y que aunque gran parte de los mismos mantienen relaciones sexuales siendo solteros, utilizan métodos anticonceptivos regulares y muy pocos recurren a AE. Casi todos los estudiantes son católicos, pero la mayoría están de acuerdo con su uso y lo recomendaría a otras personas y se observa que no tienen mayores prejuicios so-ciales, ni religiosos en torno a la contracepción de urgencia. Un alto porcentaje conoce que el LNG se utiliza para AE y los aspectos generales sobre ésta, pero desconocen aquello de más complejidad. Todos los estudiantes que han utilizado la anticoncepción post hoc, han logrado evitar una gestación no deseada y coinciden la mayoría que es un método absolutamente eficaz
Resumo:
Institutions need to be aware of the complex way in which professional trajectories are built upon in order to offer under graduate and graduate students different possibilities for developing needed competences to display in practice. This paper focuses on the study2 conducted by ESEPF on its former students of Social Education, through a written questionnaire analysing different parameters of their professional transitions, from entrance at training, first job and entrance on the labour market, present work situations, developed competences and perceptions of the Social Educator role on Portuguese Society, among others. Results will be presented and discussed. Particular focus will be given on the specific role of Social Education and its distinctive features towards other “social work” professions.
Resumo:
Antigone (Sofokleen mukaan) 3-osainen värirunoelma orkesterille op. 23 (1921–22) 4334/4431/12/2/cel/str. (0#/b) Sijainti Kansalliskirjastossa: COLL. 592.2 Teoksen sijainti muissa arkistoissa: Helsingin kaupunginarkisto, HKO käsikirjoituspartituurit. Käsikirjoitus, lyijykynä. FIMIC 286 Teostiedot: Osat: I Antigonen kuolinuhri veljelleen II Tyrannin tuomio III Antigonen kuolema KE 16. 11. 1922 Helsinki. HKO, joht. Toivo Haapanen. SSL:n viides vuosikonsertti. Kustanne: Fennica Gehrman, vuokramateriaali. Levytys: ”Väinö Raitio. Orchestral works. Ondine ODE 790-2 (1992) (RSO, Jukka-Pekka Saraste) Kesto: 25’ Synopsis: Oidipuksen tytär Antigone uhmaa Theban tyrannihallitsijan Kreonin tahtoa suorittamalla uhrimenot kaksintaistelussa kuolleen veljens puolesta. Tästä suuttuneena Kreon määrää Antigonen muurattavaksi elävältä ovettomaan ja ikkunattomaan kammioon, mutta katuu päätöstään heti kuultuaan tietäjän ennustavan hänelle teon johdosta synkkää kohtaloa. Antigone kuitenkin tekee itsemurhan ennen kuin Kreon ehtii häntä vapauttamaan, ja tietäjän ennustama murhenäytelmä toteutuu, sillä Antigonen kuolema aiheuttaa kaksi muutakin itsemurhaa. Sekä Kreonin oma poika, joka oli Antigonen kihlattu että Eurydike, Kreonin vaimo riistävät tapahtumien johdosta itseltään hengen. (Sofokles 1910.) Raition Antigone noudattaa osiensa otsikoiden puolesta Sofokleen murhenäytelmän päätapahtumia, mutta varsinaista tarkkaa ohjelmaa teoksen partituurissa ei ole nähtävissä. Näytelmän tapahtumat toimivat pikemminkin teoksen yleistunnelman lähteinä. Omakätinen puhtaaksikirjoitus. Orkesteripartituuri. Sivumäärä: 105 + 2 (kansi ja tausta) + 1 (tyhjä). Sivunumerot: [1.] 2.–19. [20.] 21.–51. [52.] 53.–105. [Ruskea muste, VR] Paperi: Ensimmäinen arkki tunnistamaton 28. Muut: FM 28. Käsikirjoitus: Ruskea muste, VR. Korjauksia tehty raaputtamalla. Lisyksiä [violetti puukynä, VR]. Harjoitusnumerot: 1–9 [I osa] 10–21 [II osa] 22–42 [III osa] [violetti/sininen puukynä, ympyröity punaisella puukynällä, VR]. Osien kestot merkitty niiden loppuun [ruskea muste, VR]. Kansilehti: Antigone / (Sofokleen mukaan) / 3-osainen värirunoelma suurelle orkesterille. / Väinö Raitio /op. 23 [Ruskea muste, VR]. Kansilehden takana: Orchestra: / Fl. gr. 1.2., Fl. Picc. 1.2., Ob. 1.2., Corn. Inglese, Clar. 1.2., / Clarinetto basso, Fag. 1.2.3., Contrafagotto, Corni 1.2.3.4. in F / Trombe 1.2.3.4., Tromboni 1.2.3. Basso Tuba, / Celesta, Arpa 1.2. / Trianglo, Campanelli, Tamburo, Timpani, Piatti, Gr. Cassa, Tamtam, Campani E,c,d,e,f,g. / 16 Viol. 1., 14 Viol. 2., 12 Viole, / 10 Celli, 8 Contrabassi. [ruskea muste, VR]. S1: Antigone / Väinö Raitio / op. 23 / I. – Antigonen kuolinuhri veljelleen. / Lento espressivo. [ruskea muste, VR]. S20: II. – Tyrannin tuomio. / Andante moderato (1/4 = 60) [ruskea muste, VR]. S52: III. – Antigonen kuolema. / Adagio non troppo (1/8 = 66) S105: 1921-22. [ruskea muste, VR]. Viimeisellä sivulla A3. [lyijykynä, tk].
Resumo:
How can we understand the gender logic underpinning the welfare states/systems of East Asia? Does the comparative literature, which has largely been concerned with western Welfare states, whether in The Three Worlds of Welfare Capitalism (Esping-Andersen 1990), or in gender-based analysis of the male breadwinner model (Lewis 1992, 2001, 2006), have anything to offer in understanding the gender assumptions underpinning East Asian welfare states? Are the welfare systems of East Asian countries distinctive, with Confucian assumptions hidden beneath the surface commitment to gender equality? We will use the (mainly western) comparative literature, but argue that Confucian influences remain important, with strong assumptions of family, market and voluntary sector responsibility rather than state responsibility, strong expectations of women’s obligations, without compensating rights, a hierarchy of gender and age, and a highly distinctive, vertical family structure, in which women are subject to parents-in-law. In rapidly changing economies, these social characteristics are changing too. But they still put powerful pressures on women to conform to expectations about care, while weakening their rights to security and support. Nowhere do welfare states promises bring gender equality in practice. Even in Scandinavian countries women earn less, care more, and have less power than men. We shall compare East Asian countries (Japan, Korea, Taiwan where possible) with some Western ones, to argue that some major comparative data (e.g. OECD) show the extreme situation of women in these countries. Some fine new qualitative studies give us a close insight into the experience of mothers, including lone and married mothers, which help us to understand how far the gender assumptions of welfare states are from Scandinavia’s dual earner model. There are signs of change in society as well as in economy, and room for optimism that women’s involvement in social movements and academic enquiry may be challenging Confucian gender hierarchies.
Resumo:
Black-lip pearl oyster culture in French Polynesia is still based on natural spat collection from wild stocks, but new developments in hatchery technology and selective breeding are bringing substantive change to the sector.
Resumo:
Poster apresentado nas XXIII Jornadas Internacionais de Medicina Dentária do ISCSEM. Egas Moniz, Caparica, Portugal, 20-21 Março 2015
Resumo:
Poster apresentado nas XXIII Jornadas Internacionais de Medicina Dentária do ISCSEM. Egas Moniz, Caparica, Portugal, 20-21 Março 2015
Resumo:
Poster apresentado nas XXIII Jornadas Internacionais de Medicina Dentária do ISCSEM. Egas Moniz, Caparica, Portugal. 20-21 Março 2015