博士 / 國立臺灣大學 / 分子與細胞生物學研究所 / 94 / A cDNA encoding cathepsin Z (CTPZ) was cloned from a carp ovarian cDNA library. It is homologous to mammalian CTPZ. The amino acid residues important for protein folding and enzymatic activity of cysteine proteases are conserved in carp CTPZ. During oocyte maturation, cathepsin Z transcripts increased and reached peak at 8 h post-treatment of GnRH analogue by 9-folds compared to that of untreated oocytes, then declined near to the level of untreated oocytes in ovulated eggs.
Cathepsin Z was discharged from cortical granules to perivitelline space after cortical reaction and became new component of fertilization envelope. Inside the oocyte, cathepsin Z was stained in the cytoplasm surrounding the yolk granules. The recombinant cathepsin Z has an enzymatic activity toward vitellogenin, and inhibited by PMSF or E-64, a specific inhibitor of thiol protease. The potential roles of cathepsin Z in carp eggs are discussed.
| Identifer | oai:union.ndltd.org:TW/094NTU05061013 |
| Date | January 2006 |
| Creators | Chi-Min Kao, 高啟明 |
| Contributors | 黃火鍊 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 74 |
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