ISSN:
1432-2048
Keywords:
Adenosine 5′-phosphosulfate sulfotransferase
;
Chloroplasts
;
Spinacia sulfate reduction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00392000
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