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An extracellular, aminopeptidase (AMP) of a bacterial soil isolate, Aeromonas caviae T-58, was purified to eleclrophorclically homogeneity by ammonium sulfate precipitation and ion-exchange chromatography (Q-Sepharose fast flow and Mono-Q column) to 48-fold with a yield of 3.0%. The purified native...
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2007
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| LEADER | 00000njm a2000000a 4500 | ||
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| 001 | oai:repository.ui.edu.ng:123456789/4799 | ||
| 042 | |a dc | ||
| 720 | |a Abu, O. A. |e author | ||
| 720 | |a Nirasawa, S. |e author | ||
| 720 | |a Kitaoka, M. |e author | ||
| 720 | |a Hayashi, K. |e author | ||
| 260 | |c 2007 | ||
| 520 | |a An extracellular, aminopeptidase (AMP) of a bacterial soil isolate, Aeromonas caviae T-58, was purified to eleclrophorclically homogeneity by ammonium sulfate precipitation and ion-exchange chromatography (Q-Sepharose fast flow and Mono-Q column) to 48-fold with a yield of 3.0%. The purified native enzyme is a monomer and exhibited a single band with molecular weight of 32 kDa estimated by SDS/polyaciylamide-gel electrophoresis. The enzyme was inactivated by Mn2+, Co 2+, Cu2+, and Cd2+, but not affected by Ca2+ Ba2+, Zn2+, AI3+, NI2+, LI2+ Pb2+ and Mg2+. EDTA completely inhibited enzyme activity indicative of the enzyme to a metalloenzyme type. The addition of I mM Zn2+ restored 100% activity of EDTA-inhibited enzyme while I mM Co2+ restored 10% activity. However, the addition of equimolar concentrations of both metals showed a non co- catalytic effect, as residual activity reduced to 90%. The enzyme therefore possibly belongs to a catalytic family of Zn2+ metalloenzyme and does not require Ca2+ for enzymatic activation. The purified enzyme showed a high affinity for L-Leu- p-nitroanilide and valine but not with proline, glycine or alanine-pNA. | ||
| 024 | 8 | |a 1119-4308 | |
| 024 | 8 | |a Tropical Journal of Animal Science 10(1-2), pp. 31-35 | |
| 024 | 8 | |a ui_art_abu_effects_2007 | |
| 024 | 8 | |a http://ir.library.ui.edu.ng/handle/123456789/4799 | |
| 653 | |a Chelators | ||
| 653 | |a Metal ions | ||
| 245 | 0 | 0 | |a Effects of chelators and metal ions on purified leucine-specific aminopeptidase from aeromonas caviae T-58 |