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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.
1

Molecular interactions between a monoclonal antibody and a streptoccocal cell-surface protein

Van Dolleweerd, Craig John January 2002 (has links)
No description available.
2

The study of the antigenic determinants of trichosanthin.

January 1994 (has links)
by Chung Ka Kin Kenny. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 116-120). / Acknowledgments --- p.i / Abstract --- p.ii / Contents --- p.iii / Abbreviations --- p.viii / Chapter Chapter 1 --- General Introduction / Chapter 1.1 --- Chemical and Biological Properties of TCS --- p.1 / Chapter 1.1.1 --- Chemical properties --- p.2 / Chapter 1.1.2 --- Biological properties --- p.5 / Chapter 1.2 --- Structure of Antigens --- p.6 / Chapter 1.3 --- Methods Used for the Mapping of Antigenic Sites on the Protein --- p.8 / Chapter 1.4 --- Objective and Strategy of the Study of the Antigenic Determinants of TCS --- p.13 / Chapter Chapter 2 --- Materials and Methods / Chapter 2.1 --- Bacterial Strains Used --- p.15 / Chapter 2.2 --- General Techniques --- p.16 / Chapter 2.2.1 --- Extraction of DNA by phenol/chloroform --- p.16 / Chapter 2.2.2 --- Ethanol precipitation --- p.16 / Chapter 2.2.3 --- Minipreparation of plasmid --- p.16 / Chapter 2.2.4 --- Preparation of plasmid DNA using Qiagen pack 100 Cartridge --- p.17 / Chapter 2.2.5 --- Preparation of plasmid DNA using Magic´ёØ Minipreps DNA Purification kit from Promega --- p.18 / Chapter 2.2.6 --- Preparation and transformation of Escherichia coli competent cells --- p.19 / Chapter 2.2.7 --- Agarose gel electrophoresis of DNA --- p.21 / Chapter 2.2.8 --- Restriction enzyme digestion of DNA --- p.21 / Chapter 2.2.9 --- Purification of DNA fragment from agarose gel using Gene Clean® kit --- p.22 / Chapter 2.2.10 --- Ligation of insert into vector --- p.22 / Chapter 2.2.11 --- Rapid screening for the presence of plasmid by direct lysis of the bacterial colony --- p.23 / Chapter 2.2.12 --- SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE) --- p.24 / Chapter 2.2.13 --- Staining of protein in polyacrylamide gel --- p.25 / Chapter 2.2.14 --- Western blot detection of TCS --- p.25 / Chapter 2.2.15 --- Autoradiography --- p.27 / Chapter 2.3 --- Production of Recombinant Anti-TCS Fab Fragment --- p.27 / Chapter 2.3.1 --- Cloning and screening of the recombinant anti-TCS Fab fragment --- p.27 / Chapter 2.3.2 --- Expression of recombinant anti-TCS Fab fragment --- p.28 / Chapter 2.4 --- Construction of Deletion Library of pET58210 by Transposon Mediated Mutagenesis --- p.29 / Chapter 2.5 --- PCR Insertion Mapping of the Transposon Inserted Clones --- p.31 / Chapter 2.6 --- DNA Sequencing of Positive Clones After the PCR Insertion Mapping --- p.32 / Chapter 2.6.1 --- DNA sequencing reaction --- p.33 / Chapter 2.6.2 --- DNA sequencing gel casting and electrophoresis --- p.34 / Chapter 2.7 --- Computer Analysis of the DNA Sequence --- p.35 / Chapter 2.8 --- Subcloning of the Positive Clone that have been Located by DNA Sequencing --- p.35 / Chapter 2.8.1 --- Subcloning of the mutated TCS gene sequence with the Tn1000 delta end facing the N-tenninal of the TCS gene sequence --- p.36 / Chapter 2.8.2 --- Subcloning of the mutated TCS gene sequence with the Tn1000 gamma end facing the N-terminal of the TCS gene sequence --- p.37 / Chapter 2.9 --- Construction of Deletion Mutants that Exclude the 21 Amino Acids in the N-terminal of TCS --- p.39 / Chapter 2.10 --- Overexpression of Mutated TCS Protein with the T7 RNA Polymerase Driven Expression System --- p.41 / Chapter 2.11 --- Analysis of TCS Deletion mutants by Western Blotting --- p.42 / Chapter 2.12 --- Preparation of Recombinant TCS Protein --- p.42 / Chapter 2.13 --- Proteolytic and Chemical Cleavage of Recombinant TCS --- p.44 / Chapter 2.14 --- Tricine-SDS-16.5% Polyacrylamide Gel Electrophoresis --- p.45 / Chapter 2.15 --- Electroblotting Using Polyvinylidene Difluoride Membrane (PVDF) for N-terminal Determination --- p.48 / Chapter 2.16 --- Reagents and Buffers --- p.49 / Chapter 2.16.1 --- Media for bacterial culture --- p.49 / Chapter 2.16.2 --- Reagents for preparation of plasmid DNA --- p.51 / Chapter 2.16.3 --- DNA electrophoresis buffers --- p.51 / Chapter 2.16.4 --- Reagents for SDS-PAGE --- p.52 / Chapter 2.16.5 --- Reagents for Western blot --- p.53 / Chapter 2.16.6 --- Reagents for DNA sequencing --- p.54 / Chapter 2.16.7 --- Reagents for electroblotting using PVDF --- p.54 / Chapter Chapter 3 --- The Study of Antigenic Determinants of TCS by Transposon Mediated Deletion Mutagenesis / Chapter 3.1 --- Introduction --- p.55 / Chapter 3.2 --- Results --- p.56 / Chapter 3.2.1 --- Construction of deletion library of pET58210 by transposon mediated mutagenesis --- p.56 / Chapter 3.2.2 --- PCR insertion mapping of the transposon inserted clones --- p.60 / Chapter 3.2.3 --- DNA sequencing of positive clones after the PCR insertion mapping --- p.63 / Chapter 3.2.4 --- Computer analysis of the DNA sequence --- p.65 / Chapter 3.2.5 --- Expression of mutated plasmids with Tn 1000 --- p.65 / Chapter 3.2.6 --- Subcloning of the positive clones that have been characterized by DNA sequencing --- p.68 / Chapter 3.2.7 --- Overexpression of mutated TCS protein with the T7 RNA polymerase driven expression system --- p.71 / Chapter 3.2.8 --- Analysis of TCS deletion mutants by Western blotting --- p.71 / Chapter 3.2.9 --- Construction of deletion mutants that exclude the 21 amino acids in the N-terminal of TCS --- p.77 / Chapter 3.3 --- Discussion --- p.80 / Chapter Chapter 4 --- The Study of Antigenic Determinants on TCS by Chemical and Enzymatic Cleavages of TCS Protein / Chapter 4.1 --- Introduction --- p.89 / Chapter 4.2 --- Results --- p.91 / Chapter 4.2.1 --- Preparation of recombinant TCS protein --- p.91 / Chapter 4.2.2 --- Proteolytic and chemical cleavages of recombinant TCS --- p.94 / Chapter 4.2.3 --- Western blotting analysis of TCS protein fragment generated by proteolytic and chemical cleavage --- p.96 / Chapter 4.2.4 --- N-terminal determination of the antigenic TCS fragment produced by chemical cleavage --- p.100 / Chapter 4.3 --- Discussion --- p.103 / Chapter Chapter 5 --- General Discussion and Future Study / Chapter 5.1 --- General Discussion --- p.107 / Chapter 5.2 --- Future Study --- p.115 / References --- p.116
3

Studies on HIV-2 antibody mediated neutralisation, coreceptor usage and in vivo tropism /

Mörner, Andreas, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karolinska institutet, 2001. / Härtill 5 uppsatser.
4

Strategies for the induction of epitope-specific polyvalent CTL responses

Palmowski, Michael J. January 2002 (has links)
No description available.
5

Identification and Characterization of Lassa virus specific antibodies that recognize epitopes on Lassa virus recombinant proteins

January 2016 (has links)
acase@tulane.edu / The humoral arm of the adaptive immune system involves the production of antibodies by cells of the B cell lineage, which bind and in some cases neutralize or enhance infectivity of pathogens, including viruses. Humoral immune responses to each of the Lassa virus (LASV) structural proteins have been detected[1, 2]. However, there have been few efforts to perform fine structure epitope mapping of the antigenic sites recognized by LASV-specific antibodies. Murine monoclonal antibodies (MAbs) have been produced against several arenaviruses [1-4]. Some MAbs to Lassa virus proteins react broadly with arenaviruses demonstrating there may be an epitope or epitopes conserved among arenaviruses. Neutralizing antibody epitopes of LASV recognized by humans remains essentially unexplored. Therefore, my project will focus on identifying, characterizing and better understanding the antigen-antibody binding relationship of LASV structural proteins. We hypothesize that humans exposed to LASV differ quantitatively and qualitatively in their ability to produce antibodies that recognize potential binding epitopes on LASV proteins, and these differences can be explored via the identification and characterization of these epitopes using LASV recombinant proteins and synthetic peptides. We expect that a panel of unique human MAbs that bind specifically to LASV and LASV recombinant proteins will be isolated and prove to be valuable tools in characterizing the humoral response to LASV. The human MAbs must be characterized to determine how binding occurs. A fundamental understanding of mechanisms of antibody binding of LASV may have significant implications for the generation of antibody-based therapeutics / 1 / Rachael Yenni
6

Immunity and immunosuppression in the tumor-host interaction /

Petersson, Max, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst. / Härtill 8 uppsatser.
7

Trypanosoma dionisii: determinação do padrão de expressão de epítopos definidos por anticorpos monoclonais anti- Trypanosoma cruzi e estudos da invasão em linhagens celulares / Trypanosona dionisii: determination of expression and distrution of epitopes defined by monoclonal antibodies anti-Trypanosoma cruzi and invasion studies in cells lineages

Oliveira, Miriam Pires de Castro [UNIFESP] 28 May 2008 (has links) (PDF)
Made available in DSpace on 2015-07-22T20:50:54Z (GMT). No. of bitstreams: 0 Previous issue date: 2008-05-28. Added 1 bitstream(s) on 2015-08-11T03:25:44Z : No. of bitstreams: 1 Publico-10775a.pdf: 1931438 bytes, checksum: fb3a11003ba43c09b447f6ea1696ef2c (MD5). Added 1 bitstream(s) on 2015-08-11T03:25:44Z : No. of bitstreams: 2 Publico-10775a.pdf: 1931438 bytes, checksum: fb3a11003ba43c09b447f6ea1696ef2c (MD5) Publico-10775b.pdf: 1682906 bytes, checksum: f124bcedf8bfc29c924ec49679d33e2a (MD5). Added 1 bitstream(s) on 2015-08-11T03:25:44Z : No. of bitstreams: 3 Publico-10775a.pdf: 1931438 bytes, checksum: fb3a11003ba43c09b447f6ea1696ef2c (MD5) Publico-10775b.pdf: 1682906 bytes, checksum: f124bcedf8bfc29c924ec49679d33e2a (MD5) Publico-10775c.pdf: 1572132 bytes, checksum: 8590397c8daaf6f5780c084660de3854 (MD5) / Trypanosoma dionisii é um tripanosomatídeo de morcegos filogeneticamente muito próximo ao Trypanosoma cruzi, agente etiológico da Doença de Chagas que, segundo a Organização Mundial de Saúde, afeta 18 milhões de pessoas na América Latina além de ocorrer aproximadamente 300.000 novas infecções anualmente. Durante seu ciclo de vida, T. dionisii passa por diferentes formas evolutivas alternando entre hospedeiro vertebrado e invertebrado. As formas são: epimastigotas e tripomastigotas metacíclicas no hospedeiro invertebrado e tripomastigotas sanguíneas e amastigotas no hospedeiro vertebrado. As formas tripomastigotas metacíclicas são capazes de invadir e se multiplicar in vitro em diversos tipos de células de mamíferos. O presente trabalho teve como objetivo observar características da ultraestrutura da espécie, alguns aspectos de seu mecanismo de invasão e identificar possível compartilhamento de epítopos entre as espécies T. dionisii e T. cruzi através de ensaios utilizando anticorpos monoclonais anti-T. cruzi. Assim como ocorre com T. cruzi, as formas tripomastigotas metacíclicas de T. dionisii recrutam lisossomos durante a invasão da célula hospedeira e permanecem em vacúolos LAMP-1 positivos por várias horas. Nossos resultados mostraram que aproximadamente 10% das formas tripomastigotas metacíclicas LAMP-1 positivas de T. dionisii, transformam-se em amastigotas em compartimentos LAMP-1 positivos, permanecendo nestes vacúolos por até 96 horas. Além disto, o pré-tratamento da célula hospedeira com nocodazol (composto que despolimeriza microtúbulos, impedindo o recrutamento lisossomal) não alterou a invasão do parasita, enquanto o prétratamento com wortmanina (composto que inibe a invasão via PI3-quinase e invaginação de membrana) inibiu significativamente a invasão. Estes dados sugerem que a fusão lisossomal talvez não seja um evento crítico para o estabelecimento de uma infecção bem sucedida de T. dionisii. A análise da expressão de epítopos definidos por anticorpos monoclonais anti-amastigotas de T. cruzi mostra uma maior proximidade imuno-reativa entre T. dionisii e T. cruzi da cepa G, pois T. dionisii reagiu com apenas um dos anticorpos anti-T. cruzi da cepa CL testados. Quanto à ultraestrutura T. dionisii é bastante semelhante a T. cruzi, com exceção do núcleo, que em T. dionisii apresenta um característico padrão de condensação da cromatina. / TEDE / BV UNIFESP: Teses e dissertações
8

Enrichment of random peptide display libraries by antibodies to the HIV-1 envelope glycoproteins

Boneham, Steven Paul January 2001 (has links)
No description available.
9

Determination of epitopic fragments of [alpha]-momorcharin by expression of the full-length and modified cDNA in escherichia coli.

January 1994 (has links)
Leung Kwan-chi. / Thesis (Ph.D.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 215-223). / ACKNOWLEDGEMENTS --- p.i / ABSTRACT --- p.ii / ABBREVIATIONS --- p.iii / Chapter CHAPTER 1 --- INTRODUCTION --- p.1 / Chapter 1.1 --- Brief description of Momordica charantia --- p.2 / Chapter 1.2 --- Toxicity of RIPs and their potential uses in the treatment of AIDS --- p.3 / Chapter 1.3 --- General mechanism of action of RIPs --- p.6 / Chapter 1.4 --- Structure of αMMC --- p.7 / Chapter 1.5 --- "Antigenicities of αMMC, BMMC and TCS" --- p.13 / Chapter 1.6 --- "Immunosuppressive properties of the abortifacient proteins αMMC, BMMC and TCS" --- p.14 / Chapter 1.7 --- Objectives of our study --- p.15 / Chapter CHAPTER 2 --- EXPRESSION OF FULL-LENGTH αMMC cDNA --- p.20 / Chapter 2.1 --- Expression of αMMC cDNA as a fusion protein --- p.22 / Chapter 2.1.1 --- Materials and methods --- p.22 / Chapter 2.1.1.1 --- Construction of fusion vector pRIT2T/MMC --- p.22 / Chapter 2.1.1.2 --- Preparation of αMMC insert by PCR --- p.26 / Chapter 2.1.1.3 --- Cloning of αMMC cDNA into fusion vector pRIT2T --- p.27 / Chapter 2.1.1.4 --- Transformation --- p.28 / Chapter 2.1.1.5 --- DNA sequencing --- p.29 / Chapter 2.1.1.6 --- Expression of protein A-αMMC fusion cDNA --- p.30 / Chapter 2.1.1.7 --- Preparation of fusion αMMC for affinity chromatography --- p.31 / Chapter 2.1.1.8 --- Affinity chromatography of Protein A-αMMC fusion protein --- p.31 / Chapter 2.1.1.9 --- Cleavage of protein A-αMMC fusion protein by factor Xa --- p.32 / Chapter 2.1.1.10 --- SDS-PAGE analysis --- p.33 / Chapter 2.1.1.11 --- Western blot analysis --- p.33 / Chapter 2.1.1.12 --- Assay of biological activity --- p.35 / Chapter 2.1.2 --- Results --- p.37 / Chapter 2.1.2.1 --- Construction of pRIT2T/MMC --- p.37 / Chapter 2.1.2.2 --- DNA sequencing --- p.40 / Chapter 2.1.2.3 --- Expression of protein A-αMMC fusion cDNA --- p.42 / Chapter 2.1.2.4 --- Purification of protein A-αMMC fusion protein --- p.45 / Chapter 2.1.2.5 --- Cleavage of protein A-aMMC fusion protein --- p.49 / Chapter 2.1.2.6 --- Assay of biological activity --- p.49 / Chapter 2.1.3 --- Discussion --- p.51 / Chapter 2.2 --- Expression of αMMC cDNA as an unfused protein --- p.52 / Chapter 2.2.1 --- Materials and methods --- p.52 / Chapter 2.2.1.1 --- Construction of the plasmid pET/MMC --- p.52 / Chapter 2.2.1.2 --- Preparation of αMMC insert by PCR --- p.56 / Chapter 2.2.1.3 --- Enzyme digestions --- p.57 / Chapter 2.2.1.4 --- Ligation --- p.58 / Chapter 2.2.1.5 --- Transformation --- p.59 / Chapter 2.2.1.6 --- Screening for αMMC inserts --- p.59 / Chapter 2.2.1.7 --- DNA sequencing --- p.60 / Chapter 2.2.1.8 --- Expression of unfused aMMC cDNA --- p.60 / Chapter 2.2.1.9 --- SDS-PAGE analysis --- p.61 / Chapter 2.2.1.10 --- Western blot analysis --- p.62 / Chapter 2.2.1.11 --- Purification of recombinant αMMC --- p.62 / Chapter 2.2.1.12 --- Biological activity of recombinant αMMC --- p.63 / Chapter 2.2.1.13 --- Radioimmunoassay --- p.63 / Chapter 2.2.2 --- Results --- p.67 / Chapter 2.2.2.1 --- Screening of pET/MMC --- p.67 / Chapter 2.2.2.2 --- DNA sequencing --- p.69 / Chapter 2.2.2.3 --- Expression of unfused αMMC cDNA --- p.69 / Chapter 2.2.2.4 --- Radioimmunoassay --- p.72 / Chapter 2.2.2.5 --- Purification of recombinant αMMC --- p.74 / Chapter 2.2.2.6 --- Biological activity of recombinant αMMC --- p.74 / Chapter 2.2.3 --- Discussion --- p.80 / Chapter CHAPTER 3 --- EXPRESSION OF MODIFIED FORMS OF αMMC cDNA --- p.82 / Chapter 3.1 --- Expression of deletion fragments of αMMC cDNA --- p.83 / Chapter 3.1.1 --- Materials and methods --- p.83 / Chapter 3.1.1.1. --- Construction of deletion mutants --- p.83 / Chapter 3.1.1.1.1 --- Modification of pRIT2T/MMC --- p.86 / Chapter 3.1.1.1.2 --- Preparation of closed circular DNA --- p.86 / Chapter 3.1.1.1.3 --- Alpha-phosphorothioate nucleotide --- p.87 / Chapter 3.1.1.1.4 --- Exo III digestion --- p.89 / Chapter 3.1.1.1.5 --- Ligation --- p.89 / Chapter 3.1.1.1.6 --- Transformation --- p.90 / Chapter 3.1.1.1.7 --- Screening of deletion subclones --- p.91 / Chapter 3.1.1.2 --- Confirmation of sequences --- p.91 / Chapter 3.1.1.3 --- Expression of deletion mutants --- p.92 / Chapter 3.1.1.4 --- Purification of deletion mutants --- p.92 / Chapter 3.1.1.5 --- Cleavage of deletion mutants --- p.93 / Chapter 3.1.1.6 --- Subcloning of the αMMC cDNA fragments --- p.94 / Chapter 3.1.1.7 --- Expression of the unfused deletion --- p.96 / Chapter 3.1.2 --- Results --- p.97 / Chapter 3.1.2.1 --- Designation of the deletion mutants --- p.97 / Chapter 3.1.2.2 --- Screening of deletion mutants --- p.98 / Chapter 3.1.2.3 --- DNA sequencing --- p.100 / Chapter 3.1.2.4 --- Expression of deletion mutants --- p.109 / Chapter 3.1.2.5 --- Purification of the fusion fragments --- p.111 / Chapter 3.1.2.6 --- Digestion of deletion mutants by factor Xa --- p.113 / Chapter 3.1.2.7 --- Subcloning of αMMC deletion fragments --- p.115 / Chapter 3.1.2.8 --- Expression of the unfused aMMC deletion --- p.117 / Chapter 3.1.3 --- Discussion --- p.119 / Chapter 3.2 --- Expression of a chimeric αMMC/TCS cDNA --- p.121 / Chapter 3.2.1 --- Materials and methods --- p.122 / Chapter 3.2.1.1 --- Construction of the MMC/TCS chimeric plasmid --- p.122 / Chapter 3.2.1.1.1 --- Digestion of pfG104 - Preparation of GH1100 --- p.125 / Chapter 3.2.1.1.2 --- Preparation of the GH405 fragment --- p.125 / Chapter 3.2.1.1.3 --- Digestion of pACYC177 --- p.126 / Chapter 3.2.1.1.4 --- "Dephosphorylation, ligation and transformation" --- p.126 / Chapter 3.2.1.1.5 --- Confirmation of insert orientation --- p.127 / Chapter 3.2.1.1.6 --- "Preparation of a fragment without PstI, ScaI" --- p.128 / Chapter 3.2.1.1.7 --- Preparation of the 750-bp TCS fragment --- p.128 / Chapter 3.2.1.1.8 --- Ligation of the TCS fragment --- p.129 / Chapter 3.2.1.1.9 --- Cleavage of pACYC177/TCS with ScaI and PstI --- p.129 / Chapter 3.2.1.1.10 --- Preparation of the PstI/HhaI-digested αMMC --- p.130 / Chapter 3.2.1.1.11 --- Ligation of the 252-bp fragment --- p.131 / Chapter 3.2.1.1.12 --- Cloning of MMC/TCS chimeric fragment --- p.131 / Chapter 3.2.1.2 --- Expression of pET/MMC-TCS --- p.132 / Chapter 3.2.1.3 --- SDS-PAGE analysis --- p.133 / Chapter 3.2.1.4 --- Western blot analysis --- p.134 / Chapter 3.2.1.5 --- Purification of MMC-TCS chimeric protein --- p.134 / Chapter 3.2.2 --- Results --- p.135 / Chapter 3.2.2.1 --- Construction of pET/MMC-TCS --- p.135 / Chapter 3.2.2.2 --- Expression of TCS/MMC chimeric cDNA --- p.140 / Chapter 3.2.2.3 --- Purification of MMC-TCS chimeric protein --- p.142 / Chapter 3.2.2.4 --- Reactivity of MMC-TCS chimeric protein with various antisera --- p.145 / Chapter 3.2.3 --- Discussion --- p.146 / Chapter CHAPTER 4 --- SCREENING OF αMMC IMMUNO-REACTIVE FRAGMENTS FROM A RANDOM FRAGMENT LIBRARY --- p.148 / Chapter 4.1 --- Materials and methods --- p.150 / Chapter 4.1.1 --- Description of the pTOPE vector --- p.150 / Chapter 4.1.2 --- Construction of an αMMC random fragment library --- p.152 / Chapter 4.1.2.1 --- Preparation of the cDNA insert of αMMC --- p.155 / Chapter 4.1.2.1.1 --- Large scale prearation of theE plasmid MMC18p8 --- p.155 / Chapter 4.1.2.1.2 --- Digestion of the plasmid MMC18p8 with EcoRI --- p.156 / Chapter 4.1.2.1.3 --- Electro-elution --- p.157 / Chapter 4.1.2.2 --- DNase I digestion --- p.158 / Chapter 4.1.2.3 --- Fractionation of DNA fragments --- p.159 / Chapter 4.1.2.3.1 --- Electrophoresis --- p.159 / Chapter 4.1.2.3.2 --- Electro-elution --- p.160 / Chapter 4.1.2.4 --- Single dA Tailing --- p.161 / Chapter 4.1.2.5 --- Ligation --- p.162 / Chapter 4.1.2.6 --- Transformation --- p.162 / Chapter 4.1.2.7 --- Controls --- p.163 / Chapter 4.1.2.7.1 --- Full-length αMMC cDNA control --- p.163 / Chapter 4.1.2.7.2 --- T-Vector ligation control --- p.164 / Chapter 4.1.2.8 --- Storage of the fragment library --- p.164 / Chapter 4.1.3 --- Immunoscreening of the random fragment library OF αMMC --- p.165 / Chapter 4.1.3.1 --- Anti-αMMC sera --- p.165 / Chapter 4.1.3.2 --- Purification of anti-αMMC sera --- p.165 / Chapter 4.1.3.3 --- Colony lift --- p.167 / Chapter 4.1.3.4 --- Induction of expression --- p.169 / Chapter 4.1.3.5 --- Colony lysis --- p.169 / Chapter 4.1.3.6 --- Immunoscreening --- p.170 / Chapter 4.1.4 --- PCR screening of inserts --- p.170 / Chapter 4.1.5 --- Amplification of positive signals --- p.172 / Chapter 4.1.6 --- Dot blot --- p.173 / Chapter 4.1.7 --- Confirmation of positive signals by Western blotting --- p.174 / Chapter 4.1.8 --- Analysis of positive clones by DNA sequencing --- p.175 / Chapter 4.1.9 --- Analysis of 3-dimensional structure of αMMC --- p.176 / Chapter 4.1.10 --- Effect of a monoclonal anti-αMMC antibody (#A1) on ribosome-inactivating activity of aMMC --- p.176 / Chapter 4.2 --- Results --- p.178 / Chapter 4.2.1 --- Theoretical considerations --- p.178 / Chapter 4.2.2 --- Construction of a random fragment library of αMMC cDNA --- p.180 / Chapter 4.2.3 --- Screening for immuno-reactive fragments of αMMC --- p.183 / Chapter 4.2.4 --- Confirmation of positive signals by Western blotting --- p.186 / Chapter 4.2.5 --- Estimation of fragment sizes by PCR --- p.188 / Chapter 4.2.6 --- Analysis of the fragment sequences --- p.190 / Chapter 4.2.7 --- Cross-reactivity of the immuno-reactive fragments --- p.194 / Chapter 4.2.8 --- Effect of a monoclonal anti-αMMC antibody (#A1) on ribosome-inactivating activity of αMMC --- p.196 / Chapter 4.3 --- Discussion --- p.198 / Chapter CHAPTER 5 --- GENERAL DISCUSSION --- p.200 / Concluding remarks --- p.214 / REFERENCES --- p.215 / APPENDIXES GENERAL PROCEDURES --- p.224 / Chapter A.l --- DNA sequencing --- p.224 / Chapter A.2 --- Purification of DNA with Gene Clean --- p.229 / Chapter A.3 --- Purification of primers after synthesis --- p.230 / Chapter A.4 --- Purification of plasmid DNA by Magic Prep (Promega) --- p.232 / Chapter A.5 --- Large-scale preparation of plasmid DNA by QIAGEN --- p.234 / Chapter A.6 --- Lowry protein determination --- p.236 / Chapter A.7 --- Preparation of acid phenol --- p.237 / Chapter A.8 --- SDS-polyacrylamide gel electrophoresis --- p.238
10

T-cell responses to Plasmodium falciparum merozoite surface protein-1

Lee, Edwin A. M. January 2000 (has links)
No description available.

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