Abstract
Adenosine diphosphatase (ADPase) activity was solubilized with a non-ionic detergent, Tween 20, from human umbilical vessels and purified to homogeneity by diethylaminoethyl-Sepharose CL-6B, adenosine 5'-monophosphate-Sepharose 4B, and concanavalin A-Sepharose chromatography. The apparent molecular mass was 75 kDa. The purified enzyme hydrolyzed pyrophosphate bonds of nucleoside di- and triphosphates in the presence of calcium ion. It was insensitive to the adenosine triphosphatase (ATPase) inhibitors, oligomycin and ouabain, and sensitive to sodium azide. Therefore, we concluded that the ADPase activity in human umbilical vessels does not derive from ADPase degrading only ADP but from ATP diphosphohydrolase (EC 3.6.1.5). The broad substrate specificity and the sensitivity to various inhibitors and calcium ion are common to ATP diphosphohydrolase from bovine aorta. However, there might exist some structural difference around the active site, because the antiserum raised in rabbit against the bovine aorta enzyme scarcely inhibited the human umbilical enzyme.
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