碩士 / 國立臺灣大學 / 動物學系 / 85 / Protein geranylgeranyltransferase I was purified from the eyes
of shrimp Penaeus japonicus by the sequential column
chromatography on HiTrap Q, Superdex 200, Mono Q and peptide-
coupled affinity column. The purified enzyme was found to have
relative Mr of 66 kDa as estimated by SDS-PAGE. Since the active
protein geranylgeranyltransferase I from Superdex 200 was found
to have relative mass of 67 kDa, the purified enzyme was deduced
to be a monomer. Synthetic peptide KCFFL is the best substrate
fo the protein geranylgeranyltransferase I among the
investigated peptides. The optimal pH for enzyme activity is pH
8.0. The enzyme was inhibited by Mg++ and Zn++ ions at 0.05 mM
and 0.5 mM respectively. Since EDTA (I.C.50=0.00025 mM) is
inhibitory as well, the protein geranylgeranyltransferase I of
penaeus japonicus is a metaloenzyme.
| Identifer | oai:union.ndltd.org:TW/085NTU00312016 |
| Date | January 1997 |
| Creators | Lin, Ruei-Shiuan, 林睿軒 |
| Contributors | Chuang Nin-Nin, 莊寧寧 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 67 |
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