Human placental atp-diphosphohydrolase: Biochemical characterization, regulation and function

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 substrate specificity, and coincident M r and pI values o...

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Veröffentlicht in:	International journal of biochemistry 1994-03, Vol.26 (3), p.437-448
Hauptverfasser:	Kettlun, A.M., Alvarez, A., Quintar, R., Valenzuela, M.A., Collados, L., Aranda, E., Banda, A., Chayet, L., C̀hiong, M., Mancilla, M., Traverso-Cori, A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - pharmacology Adenosine Triphosphatases - metabolism Analytical, structural and metabolic biochemistry Apyrase - antagonists & inhibitors Apyrase - chemistry Apyrase - metabolism Binding, Competitive Biological and medical sciences Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology Humans Hydrolases Hydrolysis In Vitro Techniques Kinetics Lectins - pharmacology Microsomes - enzymology Molecular Weight Placenta - enzymology Platelet Aggregation - drug effects Pregnancy
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