Brunold, Christian; Suter, Marianne (1982). Intracellular localization of serine acetyltransferase in spinach leaves. Planta, 155(4), pp. 321-327. Springer 10.1007/BF00429459
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Intact chloroplasts isolated from spinach leaves by a combination of differential and Percoll density gradient centrifugation and free of mitochondrial and peroxisomal contamination contained about 35% of the total leaf serine acetyltransferase (EC 2.3.1.30) activity. No appreciable activity of the enzyme could be detected in the gradient fractions containing broken chloroplasts, mitochondria, and peroxisomes. L-cysteine added to the incubation mixture at 1 mM almost completely inhibited serine acetyltransferase activity, both of leaf and chloroplast extracts. D-cysteine was much less inhibitory. L-cystine up to 5 mM and O-acetyl-L-serine up to 10 mM had no effect on the enzyme activity. When measured at pH 8.4, the enzyme extracted from the leaves had a K m for L-serine of 2.4, the enzyme from the chloroplasts a K m of 2.8 mM.
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, Suter, Marianne |
Subjects: |
500 Science > 580 Plants (Botany) |
ISSN: |
0032-0935 |
Publisher: |
Springer |
Language: |
English |
Submitter: |
Peter Alfred von Ballmoos-Haas |
Date Deposited: |
13 Jun 2018 18:01 |
Last Modified: |
05 Dec 2022 15:08 |
Publisher DOI: |
10.1007/BF00429459 |
Uncontrolled Keywords: |
chloroplast (serine acetyltransferase); cysteine; serine acetyltransferase; spinacia |
BORIS DOI: |
10.7892/boris.107346 |
URI: |
https://boris.unibe.ch/id/eprint/107346 |
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