The Synthesis of Three AMP-Analogues: N6-(6-Aminohexyl)-adenosine 5′-Monophosphate, N6-(6-Aminohexyl)-adenosine 2′,5′-Bisphosphate, and N6-(6-Aminohexyl)-adenosine 3′,5′-Bisphosphate and Their Application as General Ligands in Biospecific Affinity Chromatography
(1974) In Eur J Biochem 47(1). p.81-89- Abstract
- Phosphorylation of 6‐chloropurine
riboside with phosphorus oxychloride and phosphorus trichloride gave a
mixture of the two isomers, 6‐chloropurine‐riboside 2′,5′‐bisphosphate
and 6‐chloropurine‐riboside 3′,5′‐bisphosphate. Reaction with
1,6‐diaminohexane followed by resolution of the isomeric mixture on a
Dowex 1‐X2 column yielded N6‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate and N6‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate.
The inhibition of several NADP+‐dependent and NAD+‐dependent dehydrogenases by N6‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate, N6‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate and N6‐(6‐aminohexyl)‐adenosine
... (More) - Phosphorylation of 6‐chloropurine
riboside with phosphorus oxychloride and phosphorus trichloride gave a
mixture of the two isomers, 6‐chloropurine‐riboside 2′,5′‐bisphosphate
and 6‐chloropurine‐riboside 3′,5′‐bisphosphate. Reaction with
1,6‐diaminohexane followed by resolution of the isomeric mixture on a
Dowex 1‐X2 column yielded N6‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate and N6‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate.
The inhibition of several NADP+‐dependent and NAD+‐dependent dehydrogenases by N6‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate, N6‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate and N6‐(6‐aminohexyl)‐adenosine
5′‐monophosphate was examined.
These three AMP‐analogues were attached
to Sepharose 4B by the cyanogen bromide method and the binding of
several NAD(P)+‐dependent enzymes were investigated. NADP+‐dependent enzymes were bound to Sepharose substituted with N6‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate, whereas NAD+‐dependent enzymes were not bound under the same conditions. Conversely, when N6‐(6‐aminohexyl)‐adenosine 5′‐monophosphate was used as the immobilised ligand only the NAD+‐dependent
enzymes were bound, as well as glucose‐6‐phosphate dehydrogenase
showing weak affinity. These observations strongly suggest that these
two immobilised analogues represent true biospecific and group‐specific
adsorbents. The enzymes were eluted with their complementary
nucleotides, NAD(H) and NADP(H). These techniques were utilised to
purify several NADP+‐dependent enzymes from a crude Candida utilis extract by chromatography on the new biospecific adsorbent. (Less)
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- author
- Brodelius, Peter ; Larsson, Per-Olof LU and Mosbach, Klaus LU
- organization
- publishing date
- 1974
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Eur J Biochem
- volume
- 47
- issue
- 1
- pages
- 9 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0016138153
- ISSN
- 0014-2956
- DOI
- 10.1111/j.1432-1033.1974.tb03670.x
- language
- English
- LU publication?
- yes
- id
- 10954d72-0f9c-495b-b86d-e98159a07fa9
- date added to LUP
- 2024-06-22 20:36:52
- date last changed
- 2024-09-16 13:19:39
@article{10954d72-0f9c-495b-b86d-e98159a07fa9, abstract = {{Phosphorylation of 6‐chloropurine <br> riboside with phosphorus oxychloride and phosphorus trichloride gave a <br> mixture of the two isomers, 6‐chloropurine‐riboside 2′,5′‐bisphosphate <br> and 6‐chloropurine‐riboside 3′,5′‐bisphosphate. Reaction with <br> 1,6‐diaminohexane followed by resolution of the isomeric mixture on a <br> Dowex 1‐X2 column yielded N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate and N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate.<br/>The inhibition of several NADP<sup>+</sup>‐dependent and NAD<sup>+</sup>‐dependent dehydrogenases by N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate, N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 3′,5′‐bisphosphate and N<sup>6</sup>‐(6‐aminohexyl)‐adenosine<br> 5′‐monophosphate was examined. <br/>These three AMP‐analogues were attached <br> to Sepharose 4B by the cyanogen bromide method and the binding of <br> several NAD(P)<sup>+</sup>‐dependent enzymes were investigated. NADP<sup>+</sup>‐dependent enzymes were bound to Sepharose substituted with N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 2′,5′‐bisphosphate, whereas NAD<sup>+</sup>‐dependent enzymes were not bound under the same conditions. Conversely, when N<sup>6</sup>‐(6‐aminohexyl)‐adenosine 5′‐monophosphate was used as the immobilised ligand only the NAD<sup>+</sup>‐dependent<br> enzymes were bound, as well as glucose‐6‐phosphate dehydrogenase <br> showing weak affinity. These observations strongly suggest that these <br> two immobilised analogues represent true biospecific and group‐specific <br> adsorbents. The enzymes were eluted with their complementary <br> nucleotides, NAD(H) and NADP(H). These techniques were utilised to <br> purify several NADP<sup>+</sup>‐dependent enzymes from a crude Candida utilis extract by chromatography on the new biospecific adsorbent.}}, author = {{Brodelius, Peter and Larsson, Per-Olof and Mosbach, Klaus}}, issn = {{0014-2956}}, language = {{eng}}, number = {{1}}, pages = {{81--89}}, publisher = {{Wiley-Blackwell}}, series = {{Eur J Biochem}}, title = {{The Synthesis of Three AMP-Analogues: <i>N</i><sup>6</sup>-(6-Aminohexyl)-adenosine 5′-Monophosphate, <i>N</i><sup>6</sup>-(6-Aminohexyl)-adenosine 2′,5′-Bisphosphate, and <i>N</i><sup>6</sup>-(6-Aminohexyl)-adenosine 3′,5′-Bisphosphate and Their Application as General Ligands in Biospecific Affinity Chromatography}}, url = {{http://dx.doi.org/10.1111/j.1432-1033.1974.tb03670.x}}, doi = {{10.1111/j.1432-1033.1974.tb03670.x}}, volume = {{47}}, year = {{1974}}, }