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Localization of adenosine 5′-phosphosulfate sulfotransferase in spinach leaves

✍ Scribed by Heinz Fankhauser; Christian Brunold

Publisher
Springer-Verlag
Year
1978
Tongue
English
Weight
418 KB
Volume
143
Category
Article
ISSN
0032-0935

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✦ Synopsis

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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