Properties and subcellular localization of adenosine diphosphatase in rat heart |
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| Authors: | J de Vente J Velema J Zaagsma |
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| Affiliation: | 1. Department of Medical Physics, Faculty of Medicine, Free University, van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands;2. Department of Medicinal Chemistry, Section Molecular Pharmacology, Free University, De Boelelaan 1083, 1081 HV Amsterdam, The Netherlands |
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| Abstract: | Some properties and subcellular localization of adenosine diphosphatase (ADPase) activity from rat heart have been investigated. The pH optimum was 7.4, maximal activity was found with 5 mM MgCl2, and the apparent Km was 20 microM. ADPase activity was strongly inhibited by NaF and AppNHp, and to a lesser extent by AMP and GppNHp. The enzyme was not inhibited by p-nitrophenylphosphate, beta-glycerophosphate, or pyridoxal phosphate. The distribution of ADPase activity in subcellular fractions obtained by differential centrifugation parallel ouabain-sensitive (Na+-K+)ATPase and 5'-nucleotidase activities, suggesting a plasma membrane-bound localization. The functional significance of ADPase in adenosine production and hemostasis is discussed. |
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| Keywords: | To whom correspondence should be addressed. |
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