Crystallization and Preliminary Crystallographic Characterization of the Copper-containing Amine Oxidase from Pea Seedlings
β Scribed by Valentina Vignevich; David M. Dooley; J.Mitchell Guss; Ian Harvey; Michele A. McGuirl; Hans C. Freeman
- Book ID
- 115625810
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 196 KB
- Volume
- 229
- Category
- Article
- ISSN
- 0022-2836
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π SIMILAR VOLUMES
Amine oxidases from Lathyrus odoratus and L. sativus were isolated and, following a three step purification, gave pink coloured proteins (l max 500 nm) which consisted of dimers of 72 kDa units each. Rabbit antiserum against the enzyme from L. odoratus cross-reacted with the enzyme from L. sativus.
## Abstract In a previous DFT study a mechanism for the reductive halfβreaction of pea seedling amine oxidase (PSAO) was suggested. In many of the suggested steps a lysine at the active site plays an important role. However, this lysine is not found in other amine oxidases. The primary aim of the p