Thesis--Catholic University of America, 1939. / Vita. "Literature cited": p. 25-26.

Thesis--Catholic University of America, 1939. / Vita. "Literature cited": p. 25-26.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1982. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Thesis (Ph. D.)--University of Hong Kong, 2006.

No description available.

No description available.

No description available.

An azavinamidium salt, [3-(Dimethylamino)-2-azaprop-2-en-l-ylidene] dimethylammonium chloride was reacted with primary amides, esters containing an ╬▒-methylene group and Grignard reagents. The reaction of this azavinamidium salt with amides and esters produced respectively, acyl amidines and enamino esters. Both of these products were produced in high yields by using relatively mild conditions. Reaction of the salt with Grignard reagents resulted in a novel synthesis of aldehydes. This aldehyde synthesis was shown to be of general utility and to proceed in high yields.

Immunochemical reagents were characterized under carefully controlled laboratory conditions using conventional high performance liquid chromatography instrumentation. The stationary phase was prepared by attaching antigen molecules to an insoluble support through a covalent linkage. Experiments were carried out by introducing antibody molecules into the mobile phase and monitoring their interaction with the stationary phase. Monoclonal antibodies were employed because of their more homogeneous properties compared to polyclonal antisera. Radioisotopes were employed to study low level adsorption on the stationary phase. Recovery experiments were carried out in which it was possible to account for all of the material introduced into the mobile phase. Antibodies were purified over a preparative scale antigen affinity column following labeling to insure high immunoreactivity. Studied under normally dissociating conditions, irreversible adsorption of picomole amounts of protein on the antigen stationary phase was greater than on other ligand modified stationary phases. This accumulation decreased with repeated use of the affinity column. The present study provides a framework for evaluation of other immunoaffinity systems and demonstrates that reproducible recovery of immunologically active material in high yield is possible. Monoclonal antibodies labeled with fluorescein were different from unlabeled molecules in binding and physical characteristics. Computer simulations were used to describe binding behavior. Although fluorescein labels improve detection sensitivity over native protein absorbance, their use in this case decreased binding affinity significantly. Heterogeneity of affinity purified fluorescein labeled and unlabeled monoclonal antibodies was examined with two dimensional gel electrophoresis. In addition to increased charge heterogeneity in the labeled antibody fragments, both light and heavy chains possessed more negative character. These results agree with each other. Fluorescein contains a carboxylic acid group, and modification of antibody light chains may interfere with binding affinity. The number and location of labels covalently attached to antibodies must be carefully controlled to obtain maximum detection sensitivity and preserve immunoreactivity.

by Kwong Tsz-kin. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1993. / Includes bibliographical references (leaves 90-96). / Chapter I. --- Abstract --- p.i / Chapter II. --- Acknowledgment --- p.ii / Chapter III. --- Table of contents --- p.iii / Chapter IV. --- List of Tables and Figures 、 --- p.iv / Chapter Chapter 1. --- Introduction --- p.1 / Chapter 1.1. --- General introduction / Chapter 1.2. --- Review of analytical methods for aluminium analysis / Chapter 1.3. --- Spectrofluorimetric determination of aluminium / Chapter 1.4. --- Project aim / Chapter Chapter 2. --- Experimental --- p.14 / Chapter 2.1. --- Apparatus / Chapter 2.2. --- Reagents & Material / Chapter 2.3. --- Procedure / Chapter 2.4. --- Treatment of data / Chapter Chapter 3. --- Results and discussion --- p.24 / Chapter 3.1. --- Optimization of experimental conditions / Chapter 3.2. --- Analytical Parameters / Chapter 3.3. --- Analytical results / Chapter Chapter 4. --- Conclusion --- p.89 / Chapter Chapter 5. --- References --- p.90 / Appendix --- p.97