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Evidence for cooperative effects in human liver arginase

Authordc.contributor.authorCarvajal Baeza, Nelson 
Authordc.contributor.authorAcoria García, Marina 
Authordc.contributor.authorRodríguez Vives, Juan Pablo 
Authordc.contributor.authorFernández Gálvez, Mireya 
Authordc.contributor.authorMartínez Winkler, Jorge 
Admission datedc.date.accessioned2018-12-20T14:52:42Z
Available datedc.date.available2018-12-20T14:52:42Z
Publication datedc.date.issued1982
Cita de ítemdc.identifier.citationBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Volumen 701, Issue 1, 1982, Pages 146-148
Identifierdc.identifier.issn01674838
Identifierdc.identifier.other10.1016/0167-4838(82)90324-7
Identifierdc.identifier.urihttp://repositorio.uchile.cl/handle/2250/157190
Abstractdc.description.abstractThe 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.
Lenguagedc.language.isoen
Sourcedc.sourceBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Keywordsdc.subjectHuman liver
Keywordsdc.subjectArginase
Keywordsdc.subjectCooperative effect
Títulodc.titleEvidence for cooperative effects in human liver arginase
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorapc
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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