Thesis (doctoral)--Lund University, 1998. / Added t.p. with thesis statement inserted. Includes bibliographical references.

Thesis (doctoral)--Lund University, 1998. / Added t.p. with thesis statement inserted. Includes bibliographical references.

by Ng Ping-chung. / Thesis (M. Phil.)--Chinese University of Hong Kong, 1991. / Includes bibliographical references. / Chapter 1. --- Introduction / Chapter 1.1 --- Natural History of the Bird and the Nest --- p.1 / Chapter 1.2 --- What is More Important in Saliva: Mucin or Proteoglycan? --- p.9 / Chapter 1.3 --- Extraction and characterization of salivary glycoprotein --- p.27 / Chapter 2. --- Materials and Methods / Chapter 2.1 --- Preparation of Swiftlet's Nest Extracts --- p.38 / Chapter 2.2 --- Chemical and Biochemical Analysis of SN extracts --- p.38 / Chapter 2.2.1 --- Chemical Analysis --- p.38 / Chapter 2.2.1.1 --- Element Analysis --- p.38 / Chapter 2.2.1.2 --- Ash and Atomic Absorption Analysis --- p.39 / Chapter 2.2.2 --- Biochemical Analysis --- p.39 / Chapter 2.2.2.1 --- Protein Determination --- p.39 / Chapter 2.2.2.2 --- Hexose Determination --- p.40 / Chapter 2.2.2.3 --- Uronic Acid Determination --- p.40 / Chapter 2.2.2.4 --- Hexosamine Determination --- p.41 / Chapter 2.2.2.5 --- Sialic Acid Determination --- p.42 / Chapter 2.2.2.6 --- Sulphate Determination --- p.42 / Chapter 2.3 --- Assay of Co-mitogenic Activity in Lymphocyte Culture --- p.43 / Chapter 2.3.1 --- Preparation of Human Peripheral Blood Lymphocytes --- p.43 / Chapter 2.3.2 --- Co-mitogenic Assay --- p.43 / Chapter 2.4 --- Effect of SN pretreatment on Concanavalin A-stimulated Blastogenic Response in Mouse Splenocytes --- p.44 / Chapter 2.4.1 --- Administration of SN extracts --- p.44 / Chapter 2.4.2 --- Preparation of Mouse Splenocytes --- p.45 / Chapter 2.4.3 --- Concanavalin A-stimulated Blastogenic Response Assay --- p.45 / Chapter 2.5 --- Characterization of SN extracts by Chromatographic Methods --- p.45 / Chapter 2.5.1 --- Gel Filtration Chromatography --- p.45 / Chapter 2.5.1.1 --- Sephadex G-200 Chromatography --- p.45 / Chapter 2.5.1.2 --- Superose-Fast Protein Liquid Chromatography --- p.46 / Chapter 2.5.2 --- Ion-exchange Chromatography --- p.46 / Chapter 2.5.2.1 --- DEAE-Sepharose --- p.46 / Chapter 2.5.2.2 --- Mono-Q FPLC --- p.46 / Chapter 2.5.3 --- Immobilized Metal Affinity Chromatography --- p.47 / Chapter 2.5.4 --- Wheat-germ lectin Sepharose Chromatography --- p.47 / Chapter 2.5.5 --- Octyl-Sepharose Chromatography --- p.47 / Chapter 2.5.6 --- Limulus Polyemus Agarose Chromatography --- p.48 / Chapter 2.5.7 --- Heparin-Agarose Chromatography --- p.48 / Chapter 2.6 --- Electrophoretic Analysis of SN extract --- p.49 / Chapter 2.6.1 --- Sodium Dodecyl Sulphate/Polyacrylamide Gel Electrophoresis --- p.49 / Chapter 2.6.2 --- Isoelectrofocusing in Polyacrylamide Gel --- p.50 / Chapter 2.6.2.1 --- Preparation of Gel --- p.50 / Chapter 2.6.2.2 --- Isoelectrofocusing Procedure --- p.51 / Chapter 2.6.2.3 --- "Fixing, Staining and Destaining" --- p.51 / Chapter 2.6.3 --- Gradient Polyacrylamide Gel Electrophoresis --- p.51 / Chapter 2.6.3.1 --- Preparation of Gradient Polyacrylamide Gel --- p.52 / Chapter 2.7 --- Enzymatic Modification of SN extracts --- p.53 / Chapter 2.7.1 --- B-glucuronidase (EC 3.2.1.31) --- p.53 / Chapter 2.7.2 --- Hyaluronidase (EC 3.2.1.35) --- p.53 / Chapter 2.7.3 --- Chondroitinase ABC (EC 4.2.2.4) --- p.54 / Chapter 2.8 --- Miscellaneous Reagents --- p.54 / Chapter 2.8.1 --- Phosphate-buffer-saline (PBS) --- p.54 / Chapter 2.8.2 --- Fetal Calf Serum (FGS) --- p.54 / Chapter 2.8.3 --- Mitogen --- p.55 / Chapter 2.3.4 --- Penicillin-Streptomycin-Fungizone Solution --- p.55 / Chapter 2.8.5 --- RPMI-1640 Medium --- p.55 / Chapter 2.8.6 --- Scintillant --- p.55 / Chapter 2.8.7 --- Trypan Blue Solution --- p.55 / Chapter 3 --- Results --- p.57 / Chapter 3.1 --- Extraction of Biologically active fractions from swiflet's nest --- p.57 / Chapter 3.2 --- Effect of SN pretreatment on Con A-stimulated Blastogenesis response in mouse splenocytes --- p.57 / Chapter 3.3 --- Chemical and Biochemical Analysis of SN extracts --- p.57 / Chapter 3.3.1 --- Atomic absorption analysis of metal elements --- p.57 / Chapter 3.3.2 --- Element analysis --- p.61 / Chapter 3.3.3 --- Biochemical analysis --- p.61 / Chapter 3.4 --- Chromatographic characterization of SN extracts --- p.67 / Chapter 3.4.1 --- Sephadex G-200 chromatography --- p.67 / Chapter 3.4.2 --- DEAE-Sepharose chromatography --- p.67 / Chapter 3.4.3 --- Immobilized Metal Affinity Chromatography --- p.73 / Chapter 3.4.4 --- Wheat-germ lectin Sepharose Chromatography --- p.73 / Chapter 3.4.5 --- Limulus Polyemus Agarose Chromatography --- p.73 / Chapter 3.4.6 --- Octyl-Sepharose Chromatography --- p.81 / Chapter 3.4.7 --- Heparin-Agarose Chromatography --- p.81 / Chapter 3.5 --- Electrophoretic Analysis of SN extract --- p.88 / Chapter 3.5.1 --- Sodium Dodecyl Sulphate/Polyacrylamide Gel Electrophoresis --- p.88 / Chapter 3.5.2 --- Isoelectrofocusing in Thin Layer of Polyacrylamide Gel --- p.88 / Chapter 3.5.3 --- Gradient Polyacrylamide Gel Electrophoresis --- p.88 / Chapter 3.6 --- Enzymatic Modification of SN extracts --- p.92 / Chapter 3.6.1 --- B-glucuronidase (EC 3.2.1.31) --- p.92 / Chapter 3.6.1.1 --- Alteration in co-mitogenic activity --- p.92 / Chapter 3.6.1.2 --- Alternation in uronic acid content --- p.92 / Chapter 3.7 --- Co-mitogenic activity of glycosaminoglycans --- p.92 / Chapter 3.8 --- Effect of heparin on the co-mitogenic activity of SNp2C fraction --- p.96 / Chapter 4 --- Discussion --- p.99 / Chapter 4.1 --- Extraction of Biologically active fraction from edible bird's nest --- p.99 / Chapter 4.2 --- Chemical and Biochemical characterization of active component(s) in SN extract --- p.100 / Chapter 4.3 --- Some mechanistic considerations --- p.107 / Chapter 4.4 --- Summary and Conclusion --- p.111 / References --- p.114

Sialic acids are involved in many cellular interactions. They can serve as an adhesion ligand or act as an inhibitor to cellular adhesion by charge repulsion or by masking potential ligands. Although sialic acids are implicated in the process of blastocyst implantation, their expression and regulation in uterine epithelium of mice have not been studied. The lectin, Sambucus nigra (SNA) specifically recognizes ��2,6-linked sialic acids, which are involved in cell recognition phenomena. It was used to probe frozen uterine sections from mice during days one through six of pregnancy. SNA staining was most intense at the apical surface of uterine epithelial cells on day one of pregnancy, decreased gradually through day four, and was undetectable by day five. The role of the steroid hormones, estrogen and progesterone, in regulating the expression of ��2,6-linked sialic acids was studied in uterine sections from mice during the estrous cycle and in ovariectomized mice given hormone replacement using SNA. SNA staining of these sections during the estrous cycle showed that the expression of ��2,6-linked sialic acids was stage dependent. Staining was most intense in uterine sections from mice in estrus, and was not detected in sections from mice in diestrus. In ovariectomized mice, staining was most intense in mice injected with estradiol alone, and no staining was evident in mice injected with progesterone alone. These results suggest that the expression of ��2,6-linked sialic acids decreases during the time of implantation and that estrogen stimulates and progesterone inhibits its expression. ��-Galactoside ��2,6-Sialyltransferase (��2,6-ST) is the enzyme that links sialic acids to Gal��1-4GlcNAc termini of N-linked oligosaccharides. In order to investigate the mechanism behind the hormonal regulation of ��2,6-linked sialic acids, the expression of ��2,6-ST was followed in uterine sections from mice during early pregnancy, during the estrous cycle, and in ovariectomized mice given hormone replacement. In-situ hybridization was performed using digoxigenin labeled RNA probes to characterize ��2,6-ST mRNA levels in uterine sections. Expression of ��2,6-ST protein was also measured in uterine sections with a polyclonal antibody against ��2,6-ST. The expression of ��2,6-ST mRNA and protein correlated well with the timing of the appearance of ��2,6-linked sialic acids. These results show that the expression of ��2,6-linked sialic acids on the surface of mouse uterine epithelium decreases at the time of implantation and furthermore, that this decrease is due to the regulation of ��2,6-ST by the steroid hormones. ��2,6-linked sialic acids may serve to inhibit cellular adhesion by creating a charge repulsion, or by masking potential binding sites. Removal of this inhibition may permit blastocyst implantation. / Graduation date: 2001

It is now generally accepted that casein is a heterogeneous material. Due to the development of more effective fractionation methods, the heterogeneity of casein is now known to be even more complicated than was indicated a few years ago. [...]

Thesis (Ph.D. (Biochemistry))--Mahidol University, 1982.

Thesis (Ph. D.)--Ohio State University, 2008. / Non-Latin script record

Thesis (Ph.D.) - University of St Andrews, May 2009.

No description available.

Thesis (doctoral)--Lund University, 1992. / Added t.p. with thesis statement inserted.