Abstract:
:A sulfotransferase isolated from the Cyanobacterium Synechococcus 6301 was found to be specific for 3'-phosphoadenosine-5'-phosphosulfate (PAPS). The molecular weight of this transferase has been estimated on a Sephadex-G-100 column to be about 58,000. The K m for PAPS was determined to be 20 μM. The pH optimum was 8.0. The thiol dithioerythritol was needed for activity; other thiols such as glutathione, cysteine, or mercaptoethanol did not catalyze this reaction. The transferase, however, could not react directly with the thiol. A heat-stable factor was needed in this reaction. This factor was purified by conventional techniques and its molecular weight was determined on a Sephadex-G-50 column to be about 11,500. The factor showed normal Michaelis-Menten behavior toward the PAPS-sulfotransferase. It has been identified as thioredoxin. The tranferase was inhibited by 3'-5'-ADP and 2'-5'-ADP; all other adenine-containing nucleotides such as 2'-AMP, 3'-AMP, 5'-AMP, ADP, and c-AMP did not influence this reaction.
journal_name
Plantajournal_title
Plantaauthors
Schmidt A,Christen Udoi
10.1007/BF00390254subject
Has Abstractpub_date
1978-01-01 00:00:00pages
239-44issue
3eissn
0032-0935issn
1432-2048journal_volume
140pub_type
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