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dc.contributor.authorPizauro, João M. [UNESP]
dc.contributor.authorCurti, Carlos
dc.contributor.authorCiancaglini, Pietro
dc.contributor.authorLeone, Francisco A.
dc.date.accessioned2014-05-27T03:23:31Z
dc.date.available2014-05-27T03:23:31Z
dc.date.issued1987-12-01
dc.identifierhttp://dx.doi.org/10.1016/0305-0491(87)90413-5
dc.identifier.citationComparative Biochemistry and Physiology -- Part B: Biochemistry and, v. 87, n. 4, p. 921-926, 1987.
dc.identifier.issn0305-0491
dc.identifier.urihttp://hdl.handle.net/11449/63818
dc.description.abstract1. 1. Solubilized and membrane-bound alkaline phosphatase showed Michaelis-Menten behavior in a wide range of different substrate concentrations. 2. 2. Membrane-bound alkaline phosphatase has a molecular weight of 130,000 and its minimum active configuration comprises two identical subunits of about 65,000. 3. 3. The two forms of the enzyme behave similarly with respect to NaCl, urea and guanidine HCl. 4. 4. Catalytic groups have pK values of about 8.5 and 9.7 for both membrane-bound and solubilized enzyme. © 1987.en
dc.format.extent921-926
dc.language.isoeng
dc.relation.ispartofComparative Biochemistry and Physiology -- Part B: Biochemistry and
dc.sourceScopus
dc.subjectalkaline phosphatase
dc.subjectdetergent
dc.subjectmacrogol derivative
dc.subjectoctoxinol
dc.subjectanimal
dc.subjectbiosynthesis
dc.subjectbone matrix
dc.subjectcartilage
dc.subjectenzyme induction
dc.subjectenzyme specificity
dc.subjectenzymology
dc.subjectisolation and purification
dc.subjectkinetics
dc.subjectmetabolism
dc.subjectmolecular weight
dc.subjectphysiology
dc.subjectrat
dc.subjectsolubility
dc.subjectAlkaline Phosphatase
dc.subjectAnimal
dc.subjectBone Matrix
dc.subjectCartilage
dc.subjectDetergents
dc.subjectEnzyme Induction
dc.subjectKinetics
dc.subjectMolecular Weight
dc.subjectOctoxynol
dc.subjectPolyethylene Glycols
dc.subjectRats
dc.subjectSolubility
dc.subjectSubstrate Specificity
dc.subjectSupport, Non-U.S. Gov't
dc.titleTriton X-100 solubilized bone matrix-induced alkaline phosphataseen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationDepartamento de Tecnologia Faculdade de Ciências Agrárias e Veterinárias-UNESP, 14870 Jaboticabal, SP
dc.description.affiliationDepartamento de Fisica e Quimica Faculdade de Ciências Farmacêuticas-USP, 14049 Ribeirâo Preto, SP
dc.description.affiliationDepartamento de Quimica Faculdade de Filosofia Ciências e Letras-USP, 14049 Ribeirão Preto, SP
dc.description.affiliationUnespDepartamento de Tecnologia Faculdade de Ciências Agrárias e Veterinárias-UNESP, 14870 Jaboticabal, SP
dc.identifier.doi10.1016/0305-0491(87)90413-5
dc.rights.accessRightsAcesso restrito
dc.identifier.scopus2-s2.0-0023073346
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Agrárias e Veterinárias, Jaboticabalpt
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