Human diadenosine triphosphate hydrolase: preliminary characterisation and comparison with the Fhit protein, a human tumour suppressor

Human platelets diadenosine triphosphatase was characterised and compared with the Fhit protein, a human tumour suppressor with diadenosine triphosphatase activity. Both enzymes exhibit similar Km, are similarly activated by Mg2+, Ca2+ and Mn2+, and inhibited by Zn2+ and suramin. However, they are d...

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Veröffentlicht in:	Acta biochimica polonica 2000-01, Vol.47 (2), p.435-441
Hauptverfasser:	Asensio, A C, Rodríguez-Ferrer, C R, Oaknin, S, Rotllán, P
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Anhydride Hydrolases - blood Acid Anhydride Hydrolases - chemistry Acid Anhydride Hydrolases - isolation & purification Acid Anhydride Hydrolases - metabolism Calcium - pharmacology Cations, Divalent - pharmacology Chromatography, Gel Chromatography, High Pressure Liquid Humans Kinetics Magnesium - pharmacology Manganese - pharmacology Neoplasm Proteins Proteins - chemistry Proteins - isolation & purification Proteins - metabolism Spectrometry, Fluorescence Zinc - pharmacology
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Zusammenfassung:	Human platelets diadenosine triphosphatase was characterised and compared with the Fhit protein, a human tumour suppressor with diadenosine triphosphatase activity. Both enzymes exhibit similar Km, are similarly activated by Mg2+, Ca2+ and Mn2+, and inhibited by Zn2+ and suramin. However, they are differentially inhibited by Fhit antibodies and exhibit differences in gel-filtration behaviour.
ISSN:	0001-527X 1734-154X
DOI:	10.18388/abp.2000_4023