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Encysted embryos of the brine shrimp Artemia contain a mixture of thiol protease inhibitors (TPI's) which appear to be important in the regulation of a cathepsin B-like protease. These TPI's were subjected to gel filtration, anion exchange chromatography, two types of cation exchange procedures (fast protein liquid chromatography and CM-cellulose chromatography) and high performance liquid chromatography (HPLC). Cation exchange chromatography of inhibitor preparations on a Mono S column fractionated six TPI peaks. Using HPLC to purify the proteins the TPI's eluted between 39% and 41% acetonitrile from a C-18 column revealing considerable hydrophobicity of each inhibitor. SDS-urea PAGE of these protease inhibitors yielded a mixture of proteins with approximate molecular weights of 4.9 and 12.3 kDa. Amino acid sequence analysis of the major protein peak showed it to be identical to human ubiquitin (4.9 kDa). It appears that extracts from dormant Artemia embryos contain a mixture of free and ubiquitin-associated low molecular weight TPI's; ubiquitin may be involved in the conformational modification of TPI's in dormant Artemia embryos. (Abstract shortened by UMI.)Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis1990 .S677. Source: Masters Abstracts International, Volume: 30-03, page: 0748. Thesis (M.Sc.)--University of Windsor (Canada), 1990.
Sonnenfeld-Karcz, Margaret J., "Purification and characterization of ubiquitin-associated and free thiol protease inhibitors from dormant Artemia embryos." (1990). Electronic Theses and Dissertations. 3243.