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L-ornithine decarboxylase from Evernia prunastri.
|Authors:||Escribano, M. Isabel ; Legaz, María Estrella|
|Publisher:||Fundación Romulo Raggio|
|Citation:||Phyton 44: 171- 177 (1984)|
|Abstract:||L-ornithine decarboxylase (EC 184.108.40.206) was 88-fold purified from E. prunastri thallus with an overall yield of 14.5%. The enzyme developed maximum activity when lichen thalli were floated on 40 mML-ornithine. Addition of cycloheximide to the ornithine-containing medium did not nullify activity. However, when chloramphenicol was added to the same medium, the loss of activity was about 90%. Two cellular sites of enzyme synthesis are postulated.|
|Appears in Collections:||(IF) Artículos|