M
Marta Mancilla
Researcher at University of Chile
Publications - 21
Citations - 459
Marta Mancilla is an academic researcher from University of Chile. The author has contributed to research in topics: Apyrase & ATPase. The author has an hindex of 12, co-authored 21 publications receiving 453 citations.
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Journal ArticleDOI
Partial Purification and Immunohistochemical Localization of ATP Diphosphohydrolase from Schistosoma mansoni IMMUNOLOGICAL CROSS-REACTIVITIES WITH POTATO APYRASE AND TOXOPLASMA GONDII NUCLEOSIDE TRIPHOSPHATE HYDROLASE
Eveline G. Vasconcelos,Sergio T. Ferreira,Tecia Maria Ulisses de Carvalho,Wanderley de Souza,A.M. Kettlun,Marta Mancilla,M. Antonieta Valenzuela,Sergio Verjovski-Almeida +7 more
TL;DR: Antibody cross-reactivities in the present work suggest that conserved epitopes from S. mansoni ATP diphosphohydrolase are present in this family of nucleotide-splitting enzymes.
Journal ArticleDOI
Properties of two apyrases from Solanum tuberosum
A.M. Kettlun,Luz Uribe,Victor Calvo,S Silva,José Luis Maldonado Rivera,Marta Mancilla,M. Antonieta,Valenzuela,Aída Traverso-Cori +8 more
TL;DR: Two homogeneous isoenzymes of apyrase from Pimpernel and Desiree varieties of Solanum tuberosum were obtained by affinity chromatography on agarose-Cibacron Blue or agaroses-ATP-phosphonate columns.
Journal ArticleDOI
Comparative subcellular distribution of apyrase from animal and plant sources. Characterization of microsomal apyrase.
M.A. Valenzuela,J. López,M. Depix,Marta Mancilla,A.M. Kettlun,L. Catalán,Mario Chiong,Jorge Garrido,Aída Traverso-Cori +8 more
TL;DR: Apyrase bound to microsomes from rat and potato tissues was characterized in its substrate specificity and effect of inhibitors, and a characteristic common to the microsomal and soluble apyrases is the stimulatory effect of a potato activator protein of soluble plant apyrase.
Journal ArticleDOI
Human placental ATP-diphosphohydrolase : biochemical characterization, regulation and function
A.M. Kettlun,A. Alvarez,R. Quintar,M.A. Valenzuela,L. Collados,E. Aranda,A. Banda,L. Chayet,Mario Chiong,Marta Mancilla,Aída Traverso-Cori +10 more
TL;DR: 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, which is supported by the direct effect on washed platelets and by its plasma membrane localization.
Journal ArticleDOI
ATPase-ADPase activities of rat placental tissue.
M. Pieber,M.A. Valenzuela,A.M. Kettlun,Marta Mancilla,E. Aranda,L. Collados,Aída Traverso-Cori +6 more
TL;DR: Calcium-stimulated ATPase-ADPase activities were studied in a microsomal fraction of rat placental tissue and the substrate analogue, 5'-(beta, gamma-methylene)triphosphate, protected both enzyme activities against all the modifying amino acid reagents tested.