Effect Of Homologous Series Of N-alkyl Sulfates And N-alkyl Trimethylammonium Bromides On Low Molecular Mass Protein Tyrosine Phosphatase Activity.

dc.creatorGranjeiro, José Mauro
dc.creatorMiranda, Marcio André
dc.creatorda Glória S T Maia, Maria
dc.creatorFerreira, Carmen Veríssima
dc.creatorTaga, Eulázio Mikio
dc.creatorAoyama, Hiroshi
dc.creatorVolpe, Pedro Luiz Onofrio
dc.date2004-Oct
dc.date2015-11-27T12:58:35Z
dc.date2015-11-27T12:58:35Z
dc.date.accessioned2018-03-29T00:59:55Z
dc.date.available2018-03-29T00:59:55Z
dc.identifierMolecular And Cellular Biochemistry. v. 265, n. 1-2, p. 133-40, 2004-Oct.
dc.identifier0300-8177
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/15543943
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/196027
dc.identifier15543943
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1296260
dc.descriptionThe effect of anionic and cationic surfactants on acid phosphatase denaturation has been extensively studied. Low molecular mass (LMr) protein tyrosine phosphatase (PTP), a key regulatory enzyme involved in many different processes in the cell, was distinctly affected by anionic (homologous series of n-alkyl sulfates (C8-C14)) and cationic (n-alkyl trimethylammonium bromides (C12-C16)) surfactants. At concentrations 10-fold lower critical micellar concentration (cmc) values, the enzyme was completely inactivated in the presence of anionic surfactants, in a process independent of the pH, and dependent on the chain length of the surfactants. Under the same conditions, the effect of cationic surfactants on the enzyme activity was pH-dependent and only at pH 7.0 full inactivation was observed at concentrations 10-fold higher cmc values. In contrast to cationic surfactants the effect of anionic surfactants on the enzyme activity was irreversible and was not affected by the presence of NaCl. Inorganic phosphate, a known competitive inhibitor of PTP, protected the enzyme against inactivation by the surfactants. Our results suggest that the inactivation of the LMr PTP by anionic and cationic surfactants involved both electrostatic and hydrophobic interactions, and that the interactions enzyme-surfactants probably occurred at or near the active site.
dc.description265
dc.description133-40
dc.languageeng
dc.relationMolecular And Cellular Biochemistry
dc.relationMol. Cell. Biochem.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectAnions
dc.subjectBiochemistry
dc.subjectBromides
dc.subjectCations
dc.subjectCattle
dc.subjectDose-response Relationship, Drug
dc.subjectHot Temperature
dc.subjectHydrogen-ion Concentration
dc.subjectKinetics
dc.subjectModels, Chemical
dc.subjectProtein Tyrosine Phosphatases
dc.subjectSodium Chloride
dc.subjectStatic Electricity
dc.subjectSulfates
dc.subjectSulfuric Acid Esters
dc.subjectSurface-active Agents
dc.subjectTime Factors
dc.titleEffect Of Homologous Series Of N-alkyl Sulfates And N-alkyl Trimethylammonium Bromides On Low Molecular Mass Protein Tyrosine Phosphatase Activity.
dc.typeArtículos de revistas


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