HUMAN PLACENTAL ATP-DIPHOSPHOHYDROLASE - BIOCHEMICAL-CHARACTERIZATION, REGULATION AND FUNCTION

dc.contributor.authorKETTLUN, AM
dc.contributor.authorALVAREZ, A
dc.contributor.authorQUINTAR, R
dc.contributor.authorVALENZUELA, MA
dc.contributor.authorCOLLADOS, L
dc.contributor.authorARANDA, E
dc.contributor.authorBANDA, A
dc.contributor.authorCHAYET, L
dc.contributor.authorCHIONG, M
dc.contributor.authorMANCILLA, M
dc.contributor.authorTRAVERSOCORI, A
dc.date.accessioned2025-01-21T01:35:40Z
dc.date.available2025-01-21T01:35:40Z
dc.date.issued1994
dc.description.abstract1. Kinetic and physico-chemical studies on human placental microsomal fraction confirmed that the ATPase and ADPase activities detected in this fraction correspond to the enzyme ATP-diphosphohydrolase or apyrase (EC 3.6.1.5). These include substrate specificity, and coincident M(r) and pI values of both ATPase-ADPase activities.
dc.description.abstract2. This enzyme hydrolyses both the free unprotonated and cation-nucleotide complex, the catalytic efficiency for the latter being considerably higher.
dc.description.abstract3. Microsomal apyrase is insensitive to ouabain and Ap5A. The highly purified enzyme was only inhibited by o-vanadate, DES and slightly by DCCD.
dc.description.abstract4. Apyrase seems to be a glycoprotein from its interaction with Concanavalin-A.
dc.description.abstract5. Preliminary studies on the essential amino acid residues suggest the participation of Arg, Lys and His residues, and discard the requirement of -SH, COO-, -OH, and probably also Tyr and Trp.
dc.description.abstract6. Two kinetic modulatory proteins of apyrase were detected in placental tissue. An activating protein was found in the soluble fraction and an inhibitory protein was loosely bound to the membranes.
dc.description.abstract7. The proposed in vivo function for apyrase is related to the inhibition of platelet aggregation due to its ADPase activity, which is supported by the direct effect on washed platelets and by its plasma membrane localization.
dc.fuente.origenWOS
dc.identifier.issn0020-711X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97708
dc.identifier.wosidWOS:A1994NC97500016
dc.issue.numero3
dc.language.isoen
dc.pagina.final448
dc.pagina.inicio437
dc.revistaInternational journal of biochemistry
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleHUMAN PLACENTAL ATP-DIPHOSPHOHYDROLASE - BIOCHEMICAL-CHARACTERIZATION, REGULATION AND FUNCTION
dc.typeartículo
dc.volumen26
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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