Inactivation of S-adenosylhomocysteine hydrolase by nucleosides
The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ar...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1985 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular - Amsterdam : Elsevier, 829(1985), 2, Seite 150-155 |
| Übergeordnetes Werk: |
volume:829 ; year:1985 ; number:2 ; pages:150-155 |
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NLEJ186896107 |
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| 520 | |a The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. | ||
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(DE-627)NLEJ186896107 (DE-599)GBVNLZ186896107 DE-627 ger DE-627 rakwb eng Inactivation of S-adenosylhomocysteine hydrolase by nucleosides 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kim, I.-Y. oth Zhang, C.-Y. oth Cantoni, G.L. oth Montgomery, J.A. oth Chiang, P.K. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 829(1985), 2, Seite 150-155 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:829 year:1985 number:2 pages:150-155 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 829 1985 2 150-155 |
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(DE-627)NLEJ186896107 (DE-599)GBVNLZ186896107 DE-627 ger DE-627 rakwb eng Inactivation of S-adenosylhomocysteine hydrolase by nucleosides 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kim, I.-Y. oth Zhang, C.-Y. oth Cantoni, G.L. oth Montgomery, J.A. oth Chiang, P.K. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 829(1985), 2, Seite 150-155 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:829 year:1985 number:2 pages:150-155 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 829 1985 2 150-155 |
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(DE-627)NLEJ186896107 (DE-599)GBVNLZ186896107 DE-627 ger DE-627 rakwb eng Inactivation of S-adenosylhomocysteine hydrolase by nucleosides 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kim, I.-Y. oth Zhang, C.-Y. oth Cantoni, G.L. oth Montgomery, J.A. oth Chiang, P.K. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 829(1985), 2, Seite 150-155 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:829 year:1985 number:2 pages:150-155 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 829 1985 2 150-155 |
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(DE-627)NLEJ186896107 (DE-599)GBVNLZ186896107 DE-627 ger DE-627 rakwb eng Inactivation of S-adenosylhomocysteine hydrolase by nucleosides 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kim, I.-Y. oth Zhang, C.-Y. oth Cantoni, G.L. oth Montgomery, J.A. oth Chiang, P.K. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 829(1985), 2, Seite 150-155 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:829 year:1985 number:2 pages:150-155 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 829 1985 2 150-155 |
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(DE-627)NLEJ186896107 (DE-599)GBVNLZ186896107 DE-627 ger DE-627 rakwb eng Inactivation of S-adenosylhomocysteine hydrolase by nucleosides 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Kim, I.-Y. oth Zhang, C.-Y. oth Cantoni, G.L. oth Montgomery, J.A. oth Chiang, P.K. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 829(1985), 2, Seite 150-155 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:829 year:1985 number:2 pages:150-155 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 829 1985 2 150-155 |
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inactivation of s-adenosylhomocysteine hydrolase by nucleosides |
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Inactivation of S-adenosylhomocysteine hydrolase by nucleosides |
| abstract |
The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. |
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The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. |
| abstract_unstemmed |
The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186896107</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707062202.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1985 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186896107</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186896107</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Inactivation of S-adenosylhomocysteine hydrolase by nucleosides</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1985</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The irreversible inactivation of S-adenosylhomocysteine hydrolase purified from hamster and bovine liver by adenosine analogs substituted in the 5' and 2 positions has been investigated in detail. 5'-Cyano-5'-deoxy-adenosine inactivates as potently as 9-β-d-arabinofuranosyladenine (Ara-A). Substitution of the Ara-A at the 2 position by halogens or deleting N at the 3 position decreases its potency. Although weak, 2',3'-dideoxy-adenosine can also inactivate the enzyme. The irreversible inactivation of the hydrolase in rat hepatocytes incubated with 2-chloroadenosine or 3-deaza-Ara-A could be demonstrated, concomitant with increases in ^3^5S-labeled S-adenosylhomocysteine and S-adenosylmethionine in the hepatocytes.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, I.-Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, C.-Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cantoni, G.L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Montgomery, J.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chiang, P.K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">829(1985), 2, Seite 150-155</subfield><subfield code="w">(DE-627)NLEJ185338283</subfield><subfield code="w">(DE-600)2209539-1</subfield><subfield code="x">0167-4838</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:829</subfield><subfield code="g">year:1985</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:150-155</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90183-9</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">829</subfield><subfield code="j">1985</subfield><subfield code="e">2</subfield><subfield code="h">150-155</subfield></datafield></record></collection>
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7.401189 |