Rapid and simple measurement of ATP-sulfurylase activity in crude plant extracts using an ATP meter for bioluminescence determination
✍ Scribed by Daniel Schmutz; Christian Brunold
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 373 KB
- Volume
- 121
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
ATP-sulfurylase (EC 2.7.7.4) catalyzes the first step in assimilatory sulfate reduction, forming adenosine 5'-phosphosulfate (APS) and pyrophosphate from ATP and SO:-. The extractable activity of ATP-sulfurylase was determined in crude extracts from Phaseolus vulgaris by measuring the formation of ATP, produced in the reverse reaction from APS and pyrophosphate, using purified luciferase and luciferin in an ATP meter. One determination can be performed per minute. The rates of ATP-sulfurylase activity determined by this method were about 25 times higher than the ones measured in the forward reaction as AP% formed from ATP and '5SOj-.