Measurement of ferredoxin-dependent sulfite reductase activity in crude extracts from leaves using O-acetyl-l-serine sulfhydrylase in a coupled assay system to measure the sulfide formed

von Arb, Christoph; Brunold, Christian (1983). Measurement of ferredoxin-dependent sulfite reductase activity in crude extracts from leaves using O-acetyl-l-serine sulfhydrylase in a coupled assay system to measure the sulfide formed. Analytical biochemistry, 131(1), pp. 198-204. Elsevier 10.1016/0003-2697(83)90155-0

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Ferredoxin-dependent sulfite reductase (EC 1.8.7.1) catalyses the reduction of sulfite to sulfide, using reduced ferredoxin as an electron donor. An assay system was developed for measuring this enzyme activity in crude extracts and broken chloroplast preparations from leaves. The assay consists of a coupled system in which the sulfide formed is used for cysteine synthesis by added O-acetyl-l-serine sulfhydrylase (EC 4.2.99.8). Cysteine thus formed is determined with ninhydrin under conditions where O-acetylserine does not react and serves as a measure for ferredoxin-dependent sulfite reductase activity. Cysteine synthesized in the assay can be determined from 10 to 200 nmol. One assay per minute can be performed.

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 16:44

Last Modified:

13 Jun 2018 16:44

Publisher DOI:

10.1016/0003-2697(83)90155-0

BORIS DOI:

10.7892/boris.107355

URI:

https://boris.unibe.ch/id/eprint/107355

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