Detection of Different Forms of O-Acetyl-L-Serine Sulfhydrylase in Mesophyll Protoplasts and Bundle Sheath Cells from Wheat and Maize Leaves

Schmutz, Daniel; Brunold, Christian (1983). Detection of Different Forms of O-Acetyl-L-Serine Sulfhydrylase in Mesophyll Protoplasts and Bundle Sheath Cells from Wheat and Maize Leaves. In: Potrykus, I.; Harms, C. T.; Hinnen, A.; Hütter, R.; King, P. J.; Shillito, R.D. (eds.) Protoplasts 1983. Experientia Supplementum: Vol. 45 (pp. 186-187). Basel: Birkhäuser 10.1007/978-3-0348-6556-2_83

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O-acetyl-L-serine sulfhydrylase is an enzyme of assi-milatory sulfate reduction. It catalyses the formation of cysteine from O-acetyl-L-serine and sulfur reduced to the thiol level. The pathway begins with the formation of adenosine 5′-phosphosulfate (APS) from ATP and SO4 via ATP sulfurylase (E. C. 2. 7. 7. 4). In C4 plants ATP sulfurylase is predominantly localized in the bundle sheath cells (1, 2), while O-acetyl-L-serine sulfhydrylase was detected in meso-phyll protoplasts and bundle sheath strands (2). We have shown that various forms of O-acetyl-L-serine sulfhydrylase exist in spinach (3) and Phaseolus vulgaris (4). These findings taken together prompted us to examine, whether different forms of the enzyme occured in mesophyll cells and bundle sheath cells of the C4 plant Zea mays. For comparison, we included wheat (Triticum aestivum), a C3 grass.

Item Type:

Book Section (Book Chapter)

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:

1023-294X

ISBN:

978-3-0348-6557-9

Series:

Experientia Supplementum

Publisher:

Birkhäuser

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

18 Jul 2018 12:30

Last Modified:

18 Jul 2018 12:30

Publisher DOI:

10.1007/978-3-0348-6556-2_83

URI:

https://boris.unibe.ch/id/eprint/118347

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