Typescript (Photocopy) Bibliography: leaves i-xii. (3rd paging sequence)

Thesis (Ph.D.)--Brown University, 2008. / Vita. Adviser: Wen-Ming Chu. Includes bibliographical references.

The properties of tubulins from Brugia malayi, B. pahangi, Nippostrongylus brasiliensis and rat brain were compared. Tubulins from all nematodes and rat brain were partially purified by polylysine agarose chromatography, those of brain also by cycles of assembly/disassembly, and all by taxol-induced assembly. The tubulins were compared with respect to concentration ($ mu$g tubulin/mg soluble protein), drugs binding and isoforms. The tubulins of B. malayi and B. pahangi were similar. However, the tubulin from these filariae were different from those of N. brasiliensis. Even larger differences were detected between the nematode tubulins and those of rat brain. However, all tubulins reacted to $ alpha$- and $ beta$-tubulin monoclonal antibodies, and had similar mobility on SDS-PAGE. Different peptide maps were obtained for N. brasiliensis tubulin compared with rat brain tubulin. Tubulins of N. brasiliensis bound more mebendazole than did those of Brugia nematodes (B$ sb{ rm max}$: pmoles/$ mu$g tubulin). The binding of benzimidazoles to nematode tubulins was much higher than to rat brain tubulin. Benzimidazole binding to brain tubulin was influenced by the degree of assembly of the tubulin. This did not appear to be the case for the nematode tubulins. In vitro translation of B. malayi mRNA resulted in two isoforms for both $ alpha$- and $ beta$-tubulins in contrast to the 4 $ alpha$- and 4-5 $ beta$-isoforms found naturally. This suggest post translational modification of tubulin may take place in B. malayi. This study has characterized some of the differences that exist between mammalian tubulins and those of nematodes on the one hand, and between the tubulins of a gastrointestinal nematode (N. brasiliensis) and those of filariae (B. malayi and B. pahangi) on the other hand.

Thesis (Ph. D.)--University of Adelaide, 1990. / Typescript (Photocopy). Includes bibliographical references (leaves i-xii. (3rd paging sequence)).

The location of structures within an organism and the chemical nature of these structures can be determined by cytochemical techniques. Further, such techniques may be used to demonstrate the presence of an enzyme or an enzyme system within the cell. This information can assist in the elucidation of metabolic pathways available to an organism. Despite the apparently large potential value of cytochemical information, few investigations of the cytochemistry of trypanosomes have been reported, and there are no reports available of studies upon cultural forms. Nigrelli (1929) utilized vital stains and osmic acid impregnation in studies on cytoplasmic inclusions in Trypanosoma diemyctli, a parasite of the American newt Diemyctylus viridescens. He noted, particularly, the rapid appearance of well-defined “primary” granules in the region of the kinetoplast and the more gradual appearance of “secondary,” or included, granules scattered throughout the cytoplasm with an increase in time, temperature, and dye concentration. Barrow (1954) in further studies on T. diemyctil made use of the enzymes ribonuclease (RNAase) and deoxyribonuclease (DNAase) to demonstrate the distribution of nucleic acids in the cytoplasmic inclusions and in the nucleus. Sen (1930) reported a technique for locating the enzyme urease within a tissue. His method depends on the action of urease contained within the cell upon urea, which is supplied externally in the test, to liberate carbon dioxide. The carbon dioxide is precipitated as cobalt carbonate. The carbonate is then converted to the sulfide, which may be detected visually as small black dots within the cell. Although Sen described the use of his procedure on both plant and animal tissues, its use has not previously been reported in work upon trypanosomes.

No description available.

Vita. / Digitized by Kansas Correctional Industries

ClC-1 is the major skeletal muscle chloride channel and is essential for re-establishing the resting membrane potential of muscle cells after an action potential has occurred. Many mutations throughout the CLCN1 gene, which codes for the CIC-1 protein, have been demonstrated via characterisation in heterologous expression systems, to be causative mutations for either Dominant Myotonia Congenita or Recessive Generalised Myotonia. Recently, increasing numbers of myotonic mutations have been found in the carboxyl tail of CIC-1, which demonstrates its importance as a domain that is essential for the normal function of CIC-1 channels. Previous studies in our laboratory defined a region of 18 amino acids in the immediate post D13 segment of rat CIC-1, essential for the expression of functional channels. / thesis (PhDBiomedicalScience)--University of South Australia, 2002.

No description available.

ClC-1 is the major skeletal muscle chloride channel and is essential for re-establishing the resting membrane potential of muscle cells after an action potential has occurred. Many mutations throughout the CLCN1 gene, which codes for the CIC-1 protein, have been demonstrated via characterisation in heterologous expression systems, to be causative mutations for either Dominant Myotonia Congenita or Recessive Generalised Myotonia. Recently, increasing numbers of myotonic mutations have been found in the carboxyl tail of CIC-1, which demonstrates its importance as a domain that is essential for the normal function of CIC-1 channels. Previous studies in our laboratory defined a region of 18 amino acids in the immediate post D13 segment of rat CIC-1, essential for the expression of functional channels. / Thesis (PhDBiomedicalScience)--University of South Australia, 2002.