Source:http://linkedlifedata.com/resource/pubmed/id/16742818
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| Predicate | Object |
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| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2010-6-25
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| pubmed:abstractText |
1. An F(-)-insensitive 3'-nucleotidase was purified from spinach leaf tissue; the enzyme hydrolysed 3'-AMP, 3'-CMP and adenosine 3'-phosphate 5'-sulphatophosphate but not adenosine 5'-nucleotides nor PP(i). The pH optimum of the enzyme was 7.5; K(m) (3'-AMP) was approx. 0.8mm and K(m) (3'-CMP) was approx. 3.3mm. 3'-Nucleotidase activity was not associated with chloroplasts. Purified Mg(2+)-dependent pyrophosphatase, free from F(-)-insensitive 3'-nucleotidase, catalysed some hydrolysis of 3'-AMP; this activity was F(-)-sensitive. 2. Adenosine 5'-sulphatophosphate kinase activity was demonstrated in crude spinach extracts supplied with 3'-AMP by the synthesis of the sulphate ester of 2-naphthol in the presence of purified phenol sulphotransferase; purified ATP sulphurylase and pyrophosphatase were also added to synthesize adenosine 5'-sulphatophosphate. Adenosine 5'-sulphatophosphate kinase activity was associated with chloroplasts and was released by sonication. 3. Isolated chloroplasts synthesized adenosine 3'-phosphate 5'-sulphatophosphate from sulphate and ATP in the presence of a 3'-nucleotide; the formation of adenosine 5'-sulphatophosphate was negligible. In the absence of a 3'-nucleotide the synthesis of adenosine 3'-phosphate 5'-sulphatophosphate was negligible, but the formation of adenosine 5'-sulphatophosphate was readily detected. Some properties of the synthesis of adenosine 3'-phosphate 5'-sulphatophosphate by isolated chloroplasts are described. 4. Adenosine 3'-phosphate 5'-sulphatophosphate, synthesized by isolated chloroplasts, was characterized by specific enzyme methods, electrophoresis and i.r. spectrophotometry. 5. Isolated chloroplasts catalysed the incorporation of sulphur from sulphate into cystine/cysteine; the incorporation was enhanced by 3'-AMP and l-serine. It was concluded that adenosine 3'-phosphate 5'-sulphatophosphate is an intermediate in the incorporation of sulphur from sulphate into cystine/cysteine.
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| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13061389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13293150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13575436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13873880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13890019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-13918439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-14214087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-14439731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-1528768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-16657565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-16657611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-4306512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-4313525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-5053247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-5073745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-5499630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-5792829,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16742818-5912361
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0264-6021
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
134
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
565-79
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| pubmed:dateRevised |
2010-9-15
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| pubmed:year |
1973
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| pubmed:articleTitle |
Adenosine 5'-sulphatophosphate kinase activity in spinach leaf tissue.
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| pubmed:affiliation |
Department of Botany, La Trobe University, Bundoora, Vic. 3083, Australia.
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| pubmed:publicationType |
Journal Article
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