Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum
AUTOR(ES)
McGowan, Roy E.
RESUMO
A procedure has been developed for the purification of amine oxidase (E.C. 1.4.3.4) from etiolated pea epicotyls (Pisum sativum cv. Little Marvel). The enzyme is sensitive to copper chelating reagents and carbonyl reagents, but is not inhibited by sulfhydryl reagents. The purified enzyme has a molecular weight of 1.85 × 105, as determined by sedimentation equilibrium centrifugation, and has been shown to be specifically stimulated by phosphate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=396743Documentos Relacionados
- Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)
- Purification and Characterization of Cytosolic NADP Specific Isocitrate Dehydrogenase from Pisum sativum1
- Differential changes in size distribution of xyloglucan in the cell walls of gravitropically responding Pisum sativum epicotyls.
- Purification and properties of nitroalkane oxidase from Fusarium oxysporum.
- Purification and properties of sulfite oxidase from human liver.