Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis)
Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide p...
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| Autor*in: |
Morton, Dougal J. [verfasserIn] Kock, Nancy [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1990 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Journal of pineal research - Oxford [u.a.] : Wiley-Blackwell, 1984, 8(1990), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:8 ; year:1990 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1600-079X.1990.tb00804.x |
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| 520 | |a Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. | ||
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10.1111/j.1600-079X.1990.tb00804.x doi (DE-627)NLEJ240010388 DE-627 ger DE-627 rakwb Morton, Dougal J. verfasserin aut Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| enzyme kinetics Kock, Nancy verfasserin aut In Journal of pineal research Oxford [u.a.] : Wiley-Blackwell, 1984 8(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926731 (DE-600)2027992-9 1600-079X nnns volume:8 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 8 1990 1 0 |
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10.1111/j.1600-079X.1990.tb00804.x doi (DE-627)NLEJ240010388 DE-627 ger DE-627 rakwb Morton, Dougal J. verfasserin aut Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| enzyme kinetics Kock, Nancy verfasserin aut In Journal of pineal research Oxford [u.a.] : Wiley-Blackwell, 1984 8(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926731 (DE-600)2027992-9 1600-079X nnns volume:8 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 8 1990 1 0 |
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10.1111/j.1600-079X.1990.tb00804.x doi (DE-627)NLEJ240010388 DE-627 ger DE-627 rakwb Morton, Dougal J. verfasserin aut Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| enzyme kinetics Kock, Nancy verfasserin aut In Journal of pineal research Oxford [u.a.] : Wiley-Blackwell, 1984 8(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926731 (DE-600)2027992-9 1600-079X nnns volume:8 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 8 1990 1 0 |
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10.1111/j.1600-079X.1990.tb00804.x doi (DE-627)NLEJ240010388 DE-627 ger DE-627 rakwb Morton, Dougal J. verfasserin aut Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| enzyme kinetics Kock, Nancy verfasserin aut In Journal of pineal research Oxford [u.a.] : Wiley-Blackwell, 1984 8(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926731 (DE-600)2027992-9 1600-079X nnns volume:8 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 8 1990 1 0 |
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10.1111/j.1600-079X.1990.tb00804.x doi (DE-627)NLEJ240010388 DE-627 ger DE-627 rakwb Morton, Dougal J. verfasserin aut Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| enzyme kinetics Kock, Nancy verfasserin aut In Journal of pineal research Oxford [u.a.] : Wiley-Blackwell, 1984 8(1990), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926731 (DE-600)2027992-9 1600-079X nnns volume:8 year:1990 number:1 pages:0 http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 8 1990 1 0 |
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Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis) |
| abstract |
Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. |
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Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. |
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Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion. |
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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">NLEJ240010388</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707101511.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120426s1990 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1111/j.1600-079X.1990.tb00804.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ240010388</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="100" ind1="1" ind2=" "><subfield code="a">Morton, Dougal J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Some Properties of Pineal Gland Hydroxyindole-O-Methyltransferase From Black Rhinoceros (Diceros bicornis)</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1990</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">Pineal glands were obtained from two young female black rhinoceri that had died as a result of postcapture trauma during a translocation exercise. Hydroxyindole-O-methyltransferase (HIOMT) from these pineal glands showed a peak activity at pH 8.2, although high activity extended over a fairly wide pH range (7.8–8.4). N-acetylserotonin was the best hydroxyindolic substrate for the enzyme, although other hydroxyindoles were methylated, the relative affinities being similar to values previously reported for bovine HIOMT. Kinetic analyses revealed that black rhinoceros HIOMT was subject to substrate inhibition by both substrates at high concentration; this observation is unlikely to have physiological significance. The catalytic mechanism was found to be ordered Bi-Bi, in which S-adenosylmethionine is the obligatory first substrate to bind to the enzyme, such binding allowing for binding of the hydroxyindolic substrate followed by catalysis, products again leaving the catalytic site in a sequential fashion.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2007</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2007||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">enzyme kinetics</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kock, Nancy</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of pineal research</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1984</subfield><subfield code="g">8(1990), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926731</subfield><subfield code="w">(DE-600)2027992-9</subfield><subfield code="x">1600-079X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:8</subfield><subfield code="g">year:1990</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1600-079X.1990.tb00804.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</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">8</subfield><subfield code="j">1990</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.4004383 |