Pizauro, João M. [UNESP]Curti, CarlosCiancaglini, PietroLeone, Francisco A.2014-05-272014-05-271987-12-01Comparative Biochemistry and Physiology -- Part B: Biochemistry and, v. 87, n. 4, p. 921-926, 1987.0305-0491http://hdl.handle.net/11449/638181. 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. © 1987.921-926engalkaline phosphatasedetergentmacrogol derivativeoctoxinolanimalbiosynthesisbone matrixcartilageenzyme inductionenzyme specificityenzymologyisolation and purificationkineticsmetabolismmolecular weightphysiologyratsolubilityAlkaline PhosphataseAnimalBone MatrixCartilageDetergentsEnzyme InductionKineticsMolecular WeightOctoxynolPolyethylene GlycolsRatsSolubilitySubstrate SpecificitySupport, Non-U.S. Gov'tArtigo10.1016/0305-0491(87)90413-5Acesso restrito2-s2.0-0023073346