dc.creatorCarafoli, Ernesto
dc.creatorZurini, Mauro
dc.creatorBenaím, Gustavo
dc.date2017-04-05T22:48:12Z
dc.date2017-04-05T22:48:12Z
dc.date1985
dc.date.accessioned2022-10-28T01:24:20Z
dc.date.available2022-10-28T01:24:20Z
dc.identifier978-1-4613-2377-8 (Online)
dc.identifier978-1-4612-9453-5 (Print)
dc.identifierDOI: 10.1007 / 978-1-4684-5679-0_7
dc.identifierhttp://hdl.handle.net/10872/15639
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4949200
dc.descriptionThe Ca2+-pumping ATPase of plasma membrane, known to exist since 1966 [13], has now been characterized as a high Ca2 + affinity enzyme, present in all likelihood in all eukaryotic plasma membranes (for a recent review, see Ref. 11). The essential properties of this enzyme, as they can be extracted from a very large number of studies, are summarized in Table I. The ATPase is perhaps less well characterized than other members of the E I, E2 class of transport ATPases like the Na + IK + -ATPase and the Ca2 + -ATPase of sarcoplasmic reticulum. For example, it is still not known whether the acyl phosphate formed during the enzyme cycle is an aspartyl phosphate. It is also not established to the satisfaction of all specialists whether the Ca2 + I ATP stoichiometry is, as indicated in Table I, always and invariably 1. Recent reviews on the ATPase have appeared, the most comprehensive being perhaps the one by Schatzmann.
dc.languageen
dc.publisherCalcium in Biological Systems
dc.relationpp 265-273;
dc.subjectCa2+
dc.subjectATPase
dc.subjectplasma membrane
dc.subjectaffinity enzyme
dc.subjectsarcoplasmic reticulum
dc.subjectacyl phosphate
dc.titleThe Purified Calcium-Pumping A TPase of Plasma Membrane Structure-Function Relationships
dc.typeArticle


Este ítem pertenece a la siguiente institución