- About
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The Global ETD Search service is a free service for researchers
to find electronic theses and dissertations. This service is
provided by the
Networked Digital Library of Theses and Dissertations.
Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
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Showing 11 to 20 of 11482 (0.033 seconds)| 11 |
Analys, design och konstruktion av en prototyp för hantering av elevdataSäll, Tommy January 2002 (has links)
No description available.
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Studia Luciliana.Marx, Friedrich, January 1882 (has links)
Inaug.-Diss.--Bonn.
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Analys, design och konstruktion av en prototyp för hantering av elevdataSäll, Tommy January 2002 (has links)
No description available.
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| 14 |
C-box containing terminus of IgA1 protease is not required for correct recognition and hydrolysis of human IgA1.Lin, Hsien-chang 17 July 2008 (has links)
IgA1 (immunoglobulin A1) functions as an immune molecule, against microbial invaders and other pathogens, on the surface of animal and human cells, especially on the mucosal membrane. To impair the function of immunoglobulin the human immune system some bacteria secrete site-specific IgA1 proteases to cleave IgA1 at hinge region. The protease has therefore been implicated as a putative virulence factor. Although the alignment of the DNA for the proteases predicted the IgA1 protease domain and catalytic site, lack of experimental evidence hindered in both structural and functional enzymic studies. In order to elucidate and understand the exact activity, this study aims at to analyze catalytic site of IgA1 protease from H. influenza, and thus PCR was used to amplify the DNA for putative reactive site domain (1-885) and protease domain (1-2373), respectively, were cloned in pGEM-T and transferred to the expression vector, pTrcHis-A for production of the recombinant proteins. Analysis of the recombinant proteins shows that the Human IgA1 heavy chain hydrolyzed by the protease domain recombinant protein but putative reactive site. This demonstrates that protease domain is enough for protease activity. The putative reactive site domain alone is incapable in hydrolyzing Human IgA1.
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L'hépatite C à la permanence d'accès aux soins de santé du CHU de Nantes du dépistage à la prise en charge des patients en situation de précarité /Boudeau-Charruau, Bérangère Agard, Christian. January 2005 (has links) (PDF)
Thèse d'exercice : Médecine. Médecine générale : Université de Nantes : 2005. / Bibliogr. f. 127-135 [61 réf.].
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Theoretical modeling of electron transfer rates between cytochrome c and small transition metal complexes a thesis presented to the faculty of the Graduate School, Tennessee Technological University /Pathirathne, Thusitha. January 2009 (has links)
Thesis (M.S.)--Tennessee Technological University, 2009. / Title from title page screen (viewed on Mar. 12, 2010). Bibliography: leaves 89-95.
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Studia LucilianaMarx, Friedrich, January 1882 (has links)
Inaug.-Diss.--Bonn.
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Towards an HCV vaccine /Ward, Scott Matthew. January 2001 (has links) (PDF)
Thesis (Ph. D.)--University of Queensland, 2002. / Includes bibliographical references.
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Studies toward the asymmetric total synthesis of mitomycin CpdnChen, Wei, January 2003 (has links)
Thesis (Ph. D.)--Ohio State University, 2003. / Title from first page of PDF file. Document formatted into pages; contains xiii, 266 p.: ill. Includes abstract and vita. Advisor: Robert S. Coleman, Dept. of Chemistry. Includes bibliographical references (p. 208-222).
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The interaction of c-type cytochromes with Rhodospirillum rubrum reaction centersRickle, Gregory Kent, 1951- January 1977 (has links)
No description available.
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