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Table 1 Specific enzyme activities of PDE12

From: Enzyme assays for synthesis and degradation of 2-5As and other 2′-5′ oligonucleotides

 

Purified protein

(10−3 mmole 5′-AMP/(sec*g))

Substrate

PDE12

no enzyme

       A(pA)3

6.1 ± 0.3

0.2 ± 0.1

       A(pA)4

6.6 ± 0.5

0.1 ± 0.2

       A(pA)5

6.9 ± 0.6

0.0 ± 0.2

 

Crude extracts

(10−3 mmole 5′-AMP/(sec*g))

Substrate

PDE12

DsRed

EV

-

       A(pA)3

2.2 ± 0.2

0.8 ± 0.2

0.6 ± 0.4

0.1 ± 0.2

       A(pA)4

2.0 ± 0.4

0.6 ± 0.3

0.4 ± 0.5

0.2 ± 0.1

       A(pA)5

1.7 ± 0.3

0.4 ± 0.4

0.7 ± 0.3

0.0 ± 0.2

  1. Purified human PDE12ΔmTP-His or PDE12ΔmTP-His in HeLa cell protein extracts were incubated for 1 h at 37 °C in reactions with A(pA)3, A(pA)4 or)pA)5as substrates. The specific enzyme activities were calculated based on the chromatographic elution profiles, using the formulas outlined in the methods section. DsRed, EV and -: extracts from HeLa cells transfected with a construct encoding red-fluorescent protein, the empty-vector of pTriEx-3 Neo or mock-transfected, respectively. no enzyme: control reaction in which PDE12ΔmTP-His was omitted from the reaction. The data are provided as mean values of three replicates with ± values listing the standard error of the mean (s.e.m.)
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BMC Biochemistry

ISSN: 1471-2091

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