碩士 / 國立臺灣大學 / 動物學系 / 81 / A heat stable, small (apparant molecular mass 15 kDa) glyco-
protein was purified as beta-galactosidase activator protein
from the hepatopancreas of shrimp (Penaeus japonicus) with a
specific activity of 406 units／mg by using a combination of
DE-52 anionic exchange chromatography, Con A chromatography and
RP-C4 h.p.l.c. This activator protein stimulates beta-
galactosidase activi- ty in a pH range between 3.6 to 5 and has
an optimal pH at 4.6. Treatment with various detergents reveals
that under anionic de- tergents such as sodium taurocholate,
activator can exert its ac- tivity better, and we recommended a
concentration of 0.01﹪. In our experiment, we found that this
activator protein en- hances both shrimp and jack bean beta-
galactosidase but not alpha glucosidase or beta-glucosidase
which is characteristic for human saposin B. In addition,
activator protein shows no effects on the thermal stability of
beta-galactosidase.
| Identifer | oai:union.ndltd.org:TW/081NTU00312007 |
| Date | January 1993 |
| Creators | Chai,Chao-Ping, 翟兆平 |
| 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 | 76 |
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