Zobrazeno 1 - 10
of 98
pro vyhledávání: '"L. Chayet"'
Autor:
L. Chayet, M. Antonieta Valenzuela, Marta Mancilla, Aída Traverso-Cori, L. Collados, A.M. Kettlun, Mario Chiong, Lorena García
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 117:135-142
Periplasmic 5'-nucleotidase from Escherichia coli, in addition to the monophosphoesterase activity has a diphosphohydrolase activity, acting on nucleoside di- and triphosphates. We proposed that the monophosphoesterase and diphosphohydrolase activiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4848509b5a59bb0414bca51f6033a3d6
https://doi.org/10.1016/s0305-0491(96)00258-1
https://doi.org/10.1016/s0305-0491(96)00258-1
Autor:
Aída Traverso-Cori, A. Alvarez, Marta Mancilla, Lorena García, L. Collados, M.A. Valenzuela, S. Sandoval, L. Chayet, A.M. Kettlun
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 28:591-599
Ecto-nucleotidases may have a role in the regulation of purinoceptor-mediated responses. ATP-diphosphohydrolase or apyrase has been described as an ecto-nucleotidase, which is characterized by a low specificity for its substrates and bivalent cations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da52e0a4c0c55fa275eb4854d01564f
https://doi.org/10.1016/1357-2725(95)00153-0
https://doi.org/10.1016/1357-2725(95)00153-0
Autor:
L. Collados, Lorena García, Aída Traverso-Cori, A. Alvarez, Marta Mancilla, Mauricio Galleguillos, M.A. Valenzuela, L. Chayet, A.M. Kettlun
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 28:75-79
ATP-diphosphohydrolase (or apyrase) hydrolyses nucleoside di- and triphosphates in the presence of millimolar concentration of divalent cations. It is insensitive towards sulfhydryl and aliphatic hydroxyl-selective reagents and to specific inhibitors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0729a47b95d84e3033bb68a73cfb376c
https://doi.org/10.1016/1357-2725(95)00114-x
https://doi.org/10.1016/1357-2725(95)00114-x
Autor:
R. Quintar, A.M. Kettlun, Aída Traverso-Cori, A. Banda, L. Chayet, A. Alvarez, L. Collados, Marta Mancilla, M.A. Valenzuela, Mario Chiong, E. Aranda
Publikováno v:
International Journal of Biochemistry. 26:437-448
1. 1. 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 substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3056d6639d5cd715f4f4d6b583614a80
https://doi.org/10.1016/0020-711x(94)90065-5
https://doi.org/10.1016/0020-711x(94)90065-5
Autor:
L, Chayet, L, Collados, A M, Kettlun, E, Campos, A, Traverso-Cori, L, García, M A, Valenzuela
Publikováno v:
Research communications in molecular pathology and pharmacology. 96(1)
The human placental microvillar membrane contains several ectoenzymes, including 5'-nucleotidase, alkaline phosphatase and ATP-diphosphohydrolase (ATP-DPH), which might be involved in the extracellular metabolism of nucleotides. The type of anchorage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dcc2373c9661c2b43e53fae89ad40d78
https://pubmed.ncbi.nlm.nih.gov/9178364
https://pubmed.ncbi.nlm.nih.gov/9178364
Autor:
Aída Traverso-Cori, Marta Mancilla, L. Chayet, L. Collados, C. G. Acevedo, Lorena García, M.A. Valenzuela, E. Aranda, A.M. Kettlun, I. Bravo
Publikováno v:
Ecto-ATPases ISBN: 9781461377290
Vasoactive properties of adenosine and ATP on placenta has been described.1 Adenosine has been associated with vasodilation and ATP has a dual effect (vasodilation and vasoconstriction) depending on the receptors to which it binds. ADP is a powerful
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c9fabf08dea7fc44682839732d2f7f8
https://doi.org/10.1007/978-1-4615-5955-9_7
https://doi.org/10.1007/978-1-4615-5955-9_7
Autor:
L. Collados, D. Miranda, M.A. Valenzuela, Aída Traverso-Cori, Lorena García, M. Galleguillos, A. Alvarez, A.M. Kettlun, Marta Mancilla, L. Chayet
Publikováno v:
Ecto-ATPases ISBN: 9781461377290
ATP-diphosphohydrolase (EC 3.6.1.5), also known as apyrase, has been found in rat mammary gland and several other animal tissuesanimal tissues1,2,3,4. The main kinetic characteristics of this enzyme are the broad specificity towards nucleoside di- an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a65201ca80be438dd8846df9b55bec5
https://doi.org/10.1007/978-1-4615-5955-9_8
https://doi.org/10.1007/978-1-4615-5955-9_8
Autor:
L. Collados, Victoria Espinosa, L. Chayet, Lorena García, M. Galleguillos, Aída Traverso-Cori, A.M. Kettlun, Jorge Garrido, Marta Mancilla, M. Antonieta Valenzuela
Publikováno v:
Scopus-Elsevier
SUMMARY Extracellular nucleotides interact with specific receptors on the cell surface and are locally metabolized by ecto-nucleotidases. Biochemical characterization of the ATPase and ADPase activities detected in rat heart sarcolemma, under conditi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e16efc3fb089a1161bf24f2064e2303
https://pubmed.ncbi.nlm.nih.gov/8866007
https://pubmed.ncbi.nlm.nih.gov/8866007
Autor:
M A, Valenzuela, A M, Kettlun, S, Sandoval, L, García, M, Mancilla, G, Neckelmann, L, Chayet, A, Alvarez, F, Cuevas, L, Collados, V, Espinosa, A, Traverso-Cori, I, Bravo, C G, Acevedo, E, Aranda
Publikováno v:
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas. 29(5)
ATP-diphosphohydrolase (apyrase. EC 3.6.1.5) has both ATPase and ADPase activity that are stimulated by bivalent metals, with Ca2+ being the most effective. The possible physiological function of this enzyme, associated with placental and renal micro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4d41442854b242670695692100bb6cf4
https://pubmed.ncbi.nlm.nih.gov/9033808
https://pubmed.ncbi.nlm.nih.gov/9033808
Autor:
M A, Valenzuela, L, Collados, A M, Kettlun, M, Mancilla, H, Lara, J, Puente, E, Aranda, L, Chayet, A, Alvarez, A, Traverso-Cori
Publikováno v:
Comparative biochemistry and physiology. B, Comparative biochemistry. 103(1)
1. 1. The purpose of this present research was to explore the possible roles of ATP-diphosphohydrolase (apyrase) in two tissues with high energetic demands during cell proliferation and differentiation. 2. 2. Changes in apyrase activities during the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::374eef2791a5b073668a5c8540b6e5fc
https://pubmed.ncbi.nlm.nih.gov/1451429
https://pubmed.ncbi.nlm.nih.gov/1451429