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The encysted embryos of Artemia franciscana contain a potentially unique cysteine protease consisting of a cathepsin L-like protease and a tightly associated protein which has been denoted as the large subunit. Whereas the small subunit has been characterized in this laboratory as a cathepsin L-like cysteine protease, the large subunit has not been studied. The dimeric cysteine protease from Artemia encysted embryos was purified to apparent homogeneity using a multi-step method involving gel filtration, anion exchange and affinity chromatography. Five isoforms were separated by fast protein liquid chromatography. The protease subunits from each isoform were isolated using reverse phase high performance liquid chromatography. Protease Lys C and cyanogen bromide treatments were used to generate fragments for N-terminal amino acid sequencing of the large subunit from the major isoform of Artemia cysteine protease. Chromatography of the Artemia cysteine protease on Mono S at pH 5.0 led to the purification of the subunits in the native state. Based on molecular and biochemical data, several possible roles for the large subunit of Artemia cysteine protease are proposed in this thesis. (Abstract shortened by UMI.)Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis1999 .P85. Source: Masters Abstracts International, Volume: 39-02, page: 0453. Adviser: Alden Warner. Thesis (M.Sc.)--University of Windsor (Canada), 2000.
Pullumbi, Ervin., "Further characterization of the large subunit of the major embryonic Artemia franciscana cysteine protease." (2000). Electronic Theses and Dissertations. 2175.