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The Synthesis of Three AMP-Analogues: N6-(6-Amino-hexyl)-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
Avdelningen for Biokemi, Kemicentrum, Lunds Universitet.ORCID-id: 0000-0001-8899-5046
Avdelningen for Biokemi, Kemicentrum, Lunds Universitet.
Avdelningen for Biokemi, Kemicentrum, Lunds Universitet.
1974 (Engelska)Ingår i: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 47, s. 81-89Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

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 Iy6-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-aminohexy1)-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 NADPf-dependent enzymes from a crude Candida utilis extract by chromatography on the new biospecific adsorbent.

Ort, förlag, år, upplaga, sidor
1974. Vol. 47, s. 81-89
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
Naturvetenskap, Biokemi
Identifikatorer
URN: urn:nbn:se:lnu:diva-610OAI: oai:DiVA.org:lnu-610DiVA, id: diva2:307340
Tillgänglig från: 2010-04-01 Skapad: 2010-04-01 Senast uppdaterad: 2017-12-12Bibliografiskt granskad

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