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- W1997764265 abstract "The 5′-nucleotidase activity isolated from calf intestinal mucosa has been resolved into three fractions by DEAE-cellulose column chromatography. One of these fractions was obtained free of nonspecific phosphatase activity and was used for further studies. This enzyme has maximal activity between pH 6.0–6.5 in Tris-acetate buffer and at 8.0 in sodium diethyl barbiturate buffer. Complete inactivation of the enzyme occurs in the presence of 0.001 m EDTA. Manganese ions enhance the activity to the greatest extent although this metal ion can be essentially replaced with Co++ or Mg++. Further studies showed a high specificity for the hydrolysis of 5′-mononucleotides. Km values determined at pH 8.0 were 5.0–5.8 × 10−5m for AMP and 5.0–8.0 × 10−5m for GMP. At pH 6.5 the Km value for AMP is in the range 14–20 × 10−5m." @default.
- W1997764265 created "2016-06-24" @default.
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- W1997764265 date "1966-05-01" @default.
- W1997764265 modified "2023-09-24" @default.
- W1997764265 title "Calf intestinal 5′-nucleotidase" @default.
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- W1997764265 doi "https://doi.org/10.1016/0003-9861(66)90354-7" @default.
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