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  • About
  • 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.
191

Cell biology studies on established glioma cell lines and clones in vitro /

Ko, Li-wen January 1979 (has links)
No description available.
192

Cytology and growth of normal and malignant tissue.

Entin, Martin A. January 1942 (has links)
No description available.
193

Changes in enzyme patterns in cultured embryonic chick heart cells

Brookman, David H. (David Hyman) January 1969 (has links)
No description available.
194

Damaging effect of poly-L-arginine on cultured human bronchial epithelial cells, 16HBE14o-.

January 2008 (has links)
Chow, Wai Ming Alison. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2008. / Includes bibliographical references (leaves 138-153). / Abstracts in English and Chinese.
195

Identification of protein interactors of dribble: a single KH-domain nucleolar protein in Drosophila.

January 2007 (has links)
Choi, Ching Gee. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2007. / Includes bibliographical references (leaves 127-132). / Abstracts in English and Chinese. / ABSTRACT --- p.i / ABSTRACT (Chinese version) --- p.iii / ACKNOWLEDGEMENTS --- p.iv / LISTS OF ABBREVIATIONS --- p.vi / LISTS OF TABLES --- p.ix / LISTS OF FIGURES --- p.x / Chapter 1. --- INTRODUCTION / Chapter 1.1 --- The nucleolus ´ؤ a major site for ribosome biogenesis --- p.1 / Chapter 1.1.1 --- Ribosome biogenesis --- p.1 / Chapter 1.1.1.1 --- Eukaryotic ribosomal RNA processing --- p.4 / Chapter 1.1.1.2 --- Ribosome assembly --- p.5 / Chapter 1.1.2 --- Trans-acting proteins in ribosome biogenesis --- p.8 / Chapter 1.1.3 --- rRNA processing and ribosome assembly are two coordinated process --- p.9 / Chapter 1.2 --- Dribble (DBE) ´ؤ an essential nucleolar RNA-binding protein --- p.11 / Chapter 1.2.1 --- DBE carries a RNA-binding KH-domain --- p.12 / Chapter 1.2.2 --- RNA-binding properties of DBE --- p.13 / Chapter 1.2.3 --- DBE is involved in rRNA processing --- p.15 / Chapter 1.2.4 --- Yeast homolog of DBE 一 Krrlp is associated with ribosome biogenesis --- p.19 / Chapter 1.3 --- Aims of Research --- p.22 / Chapter 2. --- MATERIALS AND METHODS / Chapter 2.1 --- Expression and purification of DBE protein in Escherichia coli --- p.24 / Chapter 2.1.1 --- DNA construct --- p.24 / Chapter 2.1.2 --- Bacterial culture --- p.24 / Chapter 2.1.3 --- Purification of DBE protein --- p.25 / Chapter 2.2 --- Drosophila cell culture and preparation of protein lysates --- p.27 / Chapter 2.2.1 --- Drosophila S2 cell culture --- p.27 / Chapter 2.2.2 --- Preparation of protein lysates from Drosophila cultured cells --- p.27 / Chapter 2.2.3 --- Ribonuclease A (RNase A) treatment of protein lysates from Drosophila cultured cells --- p.28 / Chapter 2.3 --- Drosophila culture and genetics --- p.28 / Chapter 2.3.1 --- Drosophila culture --- p.28 / Chapter 2.3.2 --- GAL4/UAS transgene expression in Drosophila --- p.29 / Chapter 2.4 --- Affinity pull-down --- p.29 / Chapter 2.4.1 --- Immobilization of proteins onto AminoLink Plus coupling beads --- p.29 / Chapter 2.4.2 --- Affinity pull-down using protein coupled-beads --- p.32 / Chapter 2.5 --- Trichloroacetic acid protein precipitation --- p.33 / Chapter 2.6 --- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) --- p.33 / Chapter 2.7 --- Coomassie blue staining and destaining --- p.35 / Chapter 2.8 --- Protein identification by tandem mass spectrometry --- p.35 / Chapter 2.8.1 --- In-gel trypsin digestion of protein bands --- p.35 / Chapter 2.8.2 --- Peptide extraction --- p.37 / Chapter 2.8.3 --- Desalting of digested peptides --- p.38 / Chapter 2.8.4 --- Mass spectrometric analysis of protein candidates --- p.38 / Chapter 2.9 --- Electrotransfer and Western blotting --- p.39 / Chapter 2.10 --- Sucrose gradient sedimentation --- p.41 / Chapter 2.11 --- Glutathione S-transferase (GST) pull-down assay --- p.42 / Chapter 2.11.1 --- Construction of pRSETA-GST-r̐ư̐ưأ̐ơة plasmid --- p.42 / Chapter 2.11.1.1 --- Total RNA preparation from fly heads --- p.42 / Chapter 2.11.1.2 --- DNase treatment on extracted RNA --- p.43 / Chapter 2.11.1.3 --- Reverse Transcription --- p.44 / Chapter 2.11.1.4 --- PCR amplification of DNA fragment for cloning --- p.45 / Chapter 2.11.1.5 --- Agarose gel electrophoresis --- p.47 / Chapter 2.11.2 --- Overexpression of GST and GST-RpS9 proteins --- p.47 / Chapter 2.11.3 --- GST pull-down assay --- p.48 / Chapter 2.12 --- Immunoprecipitation ofFLAG-DBE in Drosophila --- p.49 / Chapter 2.13 --- Reagents and buffers --- p.50 / Chapter 2.13.1 --- Bacterial culture medium --- p.50 / Chapter 2.13.2 --- Buffers for purification of DBE protein in Escherichia coli --- p.51 / Chapter 2.13.3 --- Reagent for preparing protein lysates from Drosophila cultured cells --- p.53 / Chapter 2.13.4 --- Reagents for Drosophila culture and genetics --- p.53 / Chapter 2.13.5 --- Buffers for immobilization of proteins onto AminoLink Plus coupling gel --- p.55 / Chapter 2.13.6 --- Buffers for affinity pull-down using protein coupled-beads --- p.56 / Chapter 2.13.7 --- Reagents for SDS-PAGE --- p.56 / Chapter 2.13.8 --- Reagent for Coomassie Blue Staining and Destaining --- p.58 / Chapter 2.13.9 --- Reagents for protein identification by tandem mass spectrometry --- p.59 / Chapter 2.13.10 --- Reagents for electrotransfer and Western blotting --- p.62 / Chapter 2.13.11 --- Reagents for sucrose gradient sedimentation --- p.63 / Chapter 2.13.12 --- Reagents for agarose gel electrophoresis --- p.64 / Chapter 2.13.13 --- Reagents for immunoprecipitation --- p.65 / Chapter 2.13.14 --- Other common buffer --- p.66 / Chapter 3. --- RESULTS / Chapter 3.1 --- Identification of DBE protein interactors by affinity pull-down --- p.67 / Chapter 3.1.1 --- Introduction --- p.67 / Chapter 3.1.2 --- Results --- p.68 / Chapter 3.1.2.1 --- Expression and purification of DBE protein in E. coli --- p.68 / Chapter 3.1.2.2 --- Affinity pull-down using DBE-coupled beads and the control using lysozyme-coupled beads --- p.70 / Chapter 3.1.2.3 --- Affinity pull-down using DBE-coupled beads and the control using heat-denatured DBE-coupled beads --- p.73 / Chapter 3.1.2.4 --- Tandem mass spectrometric identification of proteins pulled down by DBE-coupled beads --- p.75 / Chapter 3.1.2.5 --- Study of the RNA-dependence of the interactions between DBE and its interactors --- p.83 / Chapter 3.1.3 --- Discussion --- p.89 / Chapter 3.1.3.1 --- Most DBE-interactors pulled down by DBE-coupled beads were shown to be specific --- p.89 / Chapter 3.1.3.2 --- Most of the potential DBE-interactors were found in the nucleolar proteome --- p.91 / Chapter 3.1.3.3 --- Comparison of protein interactions identified in DBE and Krrlp --- p.92 / Chapter 3.1.3.4 --- The implications of DBE-interacting ribosomal proteins on the role of DBE in ribosome biogenesis --- p.94 / Chapter 3.2 --- Study of the sedimentation behavior of DBE by sucrose gradient sedimentation --- p.97 / Chapter 3.2.1 --- Introduction --- p.97 / Chapter 3.2.2 --- Results --- p.98 / Chapter 3.2.2.1 --- The sedimentation behaviors of endogenous DBE and overexpressed FLAG-DBE --- p.98 / Chapter 3.2.3 --- Discussion --- p.100 / Chapter 3.2.3.1 --- The sedimentation behaviors of endogenous DBE and overexpressed FLAG-DBE was similar --- p.100 / Chapter 3.2.3.2 --- DBE associates with a macromolecular complex --- p.101 / Chapter 3.3 --- Study of the interaction between DBE and RpS9 by GST pull-down assay --- p.103 / Chapter 3.3.1 --- Introduction --- p.103 / Chapter 3.3.2 --- Results --- p.104 / Chapter 3.3.2.1 --- The constructs for GST and GST-RpS9 expression --- p.104 / Chapter 3.3.2.2 --- Purified DBE protein was pulled down by GST-RpS9 --- p.104 / Chapter 3.3.3 --- Discussion --- p.107 / Chapter 3.3.3.1 --- Further investigations on the interaction between DBE and RpS9 --- p.107 / Chapter 3.3.3.2 --- The implications of interaction between DBE and RpS9 on ribosome biogenesis --- p.107 / Chapter 3.3.3.3 --- The RNA dependence of the interaction between RpS9 and DBE --- p.111 / Chapter 3.4 --- Study of the association between DBE and histone proteins by co-immunoprecipitation and sucrose gradient sedimentation --- p.112 / Chapter 3.4.1 --- Introduction --- p.112 / Chapter 3.4.2 --- Result --- p.113 / Chapter 3.4.2.1 --- Histone H3 was not co-immunoprecipitated with FLAG-DBE --- p.113 / Chapter 3.4.2.2 --- Histone H3 did not co-sediment with DBE in sucrose gradient sedimentation --- p.115 / Chapter 3.4.3 --- Discussion --- p.116 / Chapter 3.4.3.1 --- Association between DBE and histone H3 could not be found --- p.116 / Chapter 3.4.3.2 --- Further investigation on the association between DBE and histone proteins --- p.118 / Chapter 4. --- GENERAL DISCUSSION --- p.119 / Chapter 5. --- CONCLUSION --- p.125 / Chapter 6. --- REFERENCES --- p.127
196

The cytology of a Haliclona oculata (Demospongiae, Haplosclerida) /

Lachance, Daniel January 1985 (has links)
No description available.
197

Identification, isolation and characterization of proinsulin producing thymic cells

Palumbo, Michael O. January 2007 (has links)
The finding that more than 152 tissue-restricted antigens are expressed by thymic medullary epithelial cells is redefining the importance of thymic central tolerance induction in the prevention of autoimmune diseases. One of the tissue-restricted antigens in the thymus is proinsulin, and in both mice and humans, reduced thymic proinsulin levels have been shown to predispose to Type 1 diabetes. Using transgenic mice expressing a functional beta-Galactosidase gene under the regulation of the Ins2 promoter we have determined that between 1-3% of all medullary thymic epithelial cells express proinsulin and that these cells are frequently part of the Hassall's Corpuscles like structures in mice. Using a cross between the beta-Galactosidase expressing mice and Immortomice (expressing SV40 large T Antigen under the regulation of the MHC I promoter), we have isolated and cultured two proinsulin and two non-proinsulin producing medullary epithelial cell lines. Microarray analysis and RT-PCR analysis of the cell lines revealed the over-expression of approximately 50 genes (>4 fold or more) in the proinsulin producing lineage, versus the non proinsulin producing lineage, and approximately half the over-expressed genes can be considered tissue-restricted antigens. We do not find any evidence for chromosomal clustering of the over-expressed genes nor do we report the expression of any other pancreatic n-cell antigens or specific pancreatic proinsulin regulatory proteins (Pdx-1, Glut-2 or GCK) within the proinsulin producing cell lines but we do detect their expression in whole thymus. Our results suggest that chromosomal clustering is not a phenomenon associated with thymic tissue-restricted antigen expression and that the mechanisms allowing for thymic tissue-restricted antigen expression are not related to the expression mechanisms of such antigens in peripheral tissues.
198

Identification, isolation and characterization of proinsulin producing thymic cells

Palumbo, Michael O. January 2007 (has links)
No description available.
199

The cytology of a Haliclona oculata (Demospongiae, Haplosclerida) /

Lachance, Daniel January 1985 (has links)
No description available.
200

A cytological study of a triploid x diploid cross of Sorghum vulgare

Price, Mary Emma. January 1955 (has links)
Call number: LD2668 .T4 1955 P75 / Master of Science

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