Localization of adenosine 5′-phosphosulfate sulfotransferase in spinach leaves

Fankhauser, Heinz; Brunold, Christian (1978). Localization of adenosine 5′-phosphosulfate sulfotransferase in spinach leaves. Planta, 143(3), pp. 285-289. Springer 10.1007/BF00392000

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Roots of spinach (Spinacia oleracea L.) seedlings contained only a very low activity of adenosine 5′-phosphosulfate sulfotransferase compared to the cotyledons. Adenosine 5′-phosphosulfate sulfotransferase activity increased about tenfold in cotyledons during greening. Preparation of organelle fractions from spinach leaves by a combination of differential and isopycnic density gradient centrifugation showed that adenosine 5′-phosphosulfate sulfotransferase banded with NADP-glyceraldehyde-3-phosphate dehydrogenase, a marker enzyme for intact chloroplasts. In the fractions of peroxisomes, mitochondria and broken chloroplasts virtually no adenosine 5′-phosphosulfate sulfotransferase activity was measured. Comparison with the chloroplast enzyme NADP-glyceraldehyde-3-phosphate dehydrogenase indicates that in spinach, adenosine 5′-phosphosulfate sulfotransferase is localized almost exclusively in the chloroplasts.

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:

0032-0935

Publisher:

Springer

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

13 Jun 2018 17:59

Last Modified:

13 Jun 2018 17:59

Publisher DOI:

10.1007/BF00392000

Uncontrolled Keywords:

adenosine 5′-phosphosulfate sulfotransferase; chloroplasts; Spinacia; sulfate reduction

BORIS DOI:

10.7892/boris.107344

URI:

https://boris.unibe.ch/id/eprint/107344

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