|
type |
Journal Article |
authors |
Taniguchi, M.; Sugiyama, T. |
title |
Aspartate aminotransferase from Eleusine coracana, a C4 plant: purification, characterization, and preparation of antibody |
journal |
Arch Biochem Biophys |
Activity |
2.6.1.1 |
ui |
91053164 |
year |
(1990) |
volume |
282 |
number |
2 |
pages |
427-32. |
| |
keywords |
*Antibody Specificity |
abstract |
Aspartate aminotransferase (AspAT) isozymes from Eleusine coracana (an NAD-malic enzyme type C4 plant) were examined. Three groups of isoenzymes were identified (AspAT-1, AspAT-2, and AspAT-3). AspAT-1 (localized in the mesophyll cells) and AspAT-3 (localized in the bundle sheath cells), both of which are considered to function in the C4 acid pathway, were purified and their kinetic and physical properties studied. Both isoenzymes had a molecular mass of 80 kDa and were shown to consist of two identical 40-kDa monomers. Except for the higher affinity for aspartate and the lower activity for the forward direction (Asp----OAA) at lower pH exhibited by AspAT-3 compared with AspAT-1, the isozymes had similar kinetic properties. However they had quite different isoelectric points. Polyclonal antibodies raised against AspAT-3 preferentially cross-reacted with AspAT-3 but did show some cross-reactivity with AspAT-1. |
last changed |
2002/11/04 17:41 |
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