Date of Award
Warner, A. H.,
CC BY-NC-ND 4.0
Cysteine proteases have been found in different subcellular fractions at different stages of Artemia franciscana development, and data suggest that these enzymes may function in different ways during the developmental processes. The different sites of localization of cysteine proteases in first and second instar larvae, and their potentially different functions may be due to different isoforms of the enzyme. Results in this thesis showed that at least 5 isoforms of a cysteine protease can be resolved by isoelectric focusing and that of these proteases, CP-1 and CP-2 are dominant in the cytoplasm of embryos while CP-3, CP-4 and CP-5 are dominant in the cytoplasm of first (0-h) and second (26-h) instar larvae of Artemia franciscana. A preliminary analysis of the cysteine protease isoform pattern in the mitochondria/lysosome fraction showed a profile similar to that found in the cytoplasmic fraction. Results of isoelectric focusing of proteins purified by fast protein liquid chromatography on Mono Q showed that the cytoplasm of 0-h embryos contains six isoforms of the cysteine protease ranging from a pI 4.3 to 6.8, whereas 1st and 2nd instar larvae contain only three to four isoforms of CP with pIs of 4.5 to 5.5. These studies demonstrate that the composition of the cysteine proteases changes during development and that the different isoforms may have different functions during development. (Abstract shortened by UMI.)Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis1997 .L58. Source: Masters Abstracts International, Volume: 37-01, page: 0205. Adviser: A. H. Warner. Thesis (M.Sc.)--University of Windsor (Canada), 1997.
Liu, Yong Bo., "Characterization of major cysteine protease isoforms in embryos and larvae of Artemia franciscana." (1997). Electronic Theses and Dissertations. 1404.