Abstract
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.
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Abbreviations
- APS:
-
Adenosine 5′-phosphosulfate
- APSSTase:
-
Adenosine 5′-phosphosulfate sulfotransferase
- BSA:
-
Bovine serum albumin
- BRIJ58:
-
Polyethylene glycolmonostearylether
- DTE:
-
Dithioerythritol
- DTT:
-
Dithiothreitol
- EDTA:
-
Ethylenediaminetetraacetic acid
- ME:
-
2-Mercaptoethanol
- NADP-GPD:
-
NADP-linked glyceraldehyde-3-phosphate dehydrogenase
- PAPS:
-
Adenosine 3′-phosphate 5′-phosphate 5′-phosphosulfate
- POPOP:
-
1,4 Di [2-(5-phenyloxazolyl)]-benzene
- PPO:
-
2,5-Diphenyloxazol
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The results presented in this paper are taken from the Ph. D. thesis of H.F.
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Fankhauser, H., Brunold, C. Localization of adenosine 5′-phosphosulfate sulfotransferase in spinach leaves. Planta 143, 285–289 (1978). https://doi.org/10.1007/BF00392000
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DOI: https://doi.org/10.1007/BF00392000