Properties and subcellular localization of adenosine diphosphatase in rat heart.

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.

journal_name

Arch Biochem Biophys

authors

de Vente J,Velema J,Zaagsma J

doi

10.1016/0003-9861(84)90615-5

subject

Has Abstract

pub_date

1984-08-15 00:00:00

pages

180-7

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(84)90615-5

journal_volume

233

pub_type

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