Schmutz, Daniel; Brunold, Christian (1982). Rapid and simple measurement of ATP-sulfurylase activity in crude plant extracts using an ATP meter for bioluminescence determination. Analytical biochemistry, 121(1), pp. 151-155. Elsevier 10.1016/0003-2697(82)90569-3
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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 SO42−. 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 AP35S formed from ATP and 35SO42−.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Stress Physiology [discontinued] 08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) |
UniBE Contributor: |
Brunold, Christian |
Subjects: |
500 Science > 580 Plants (Botany) |
ISSN: |
0003-2697 |
Publisher: |
Elsevier |
Language: |
English |
Submitter: |
Peter Alfred von Ballmoos-Haas |
Date Deposited: |
13 Jun 2018 16:37 |
Last Modified: |
05 Dec 2022 15:08 |
Publisher DOI: |
10.1016/0003-2697(82)90569-3 |
BORIS DOI: |
10.7892/boris.107354 |
URI: |
https://boris.unibe.ch/id/eprint/107354 |
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