| Author | dc.contributor.author | Carvajal Baeza, Nelson | |
| Author | dc.contributor.author | Acoria García, Marina | |
| Author | dc.contributor.author | Rodríguez Vives, Juan Pablo | |
| Author | dc.contributor.author | Fernández Gálvez, Mireya | |
| Author | dc.contributor.author | Martínez Winkler, Jorge | |
| Admission date | dc.date.accessioned | 2018-12-20T14:52:42Z | |
| Available date | dc.date.available | 2018-12-20T14:52:42Z | |
| Publication date | dc.date.issued | 1982 | |
| Cita de ítem | dc.identifier.citation | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Volumen 701, Issue 1, 1982, Pages 146-148 | |
| Identifier | dc.identifier.issn | 01674838 | |
| Identifier | dc.identifier.other | 10.1016/0167-4838(82)90324-7 | |
| Identifier | dc.identifier.uri | https://repositorio.uchile.cl/handle/2250/157190 | |
| Abstract | dc.description.abstract | The reaction kinetics of human liver arginase (l-arginine amidinohydrolase, EC 3.5.3.1) in terms of arginine concentration is strikingly altered by varying the pH. Lowering the pH from the optimum (9.5) toward a more physiological value (7.5) there is a transition from hyperbolic to sigmoidal kinetics. The cooperative effects are observed in the presence and absence of the product ornithine. Dimers of arginase exhibit typical Michaelis-Menten kinetics even in the presence of ornithine. Dimer-dimer interactions are suggested to explain the kinetic properties of arginase at pH 7.5. | |
| Lenguage | dc.language.iso | en | |
| Source | dc.source | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular | |
| Keywords | dc.subject | Human liver | |
| Keywords | dc.subject | Arginase | |
| Keywords | dc.subject | Cooperative effect | |
| Título | dc.title | Evidence for cooperative effects in human liver arginase | |
| Document type | dc.type | Artículo de revista | |
| Cataloguer | uchile.catalogador | apc | |
| Indexation | uchile.index | Artículo de publicación SCOPUS | |
| uchile.cosecha | uchile.cosecha | SI | |
