Circannual variations in mevalonate utilization in frog (Rana esculenta)
1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was fo...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1990 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Comparative Biochemistry and Physiology -- Part B: Biochemistry and - Amsterdam : Elsevier, 97(1990), 3, Seite 597-600 |
| Übergeordnetes Werk: |
volume:97 ; year:1990 ; number:3 ; pages:597-600 |
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NLEJ187204403 |
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| 520 | |a 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. | ||
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(DE-627)NLEJ187204403 (DE-599)GBVNLZ187204403 DE-627 ger DE-627 rakwb eng Circannual variations in mevalonate utilization in frog (Rana esculenta) 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bruscalupi, G. oth Castellano, F. oth Trentalance, A. oth in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Amsterdam : Elsevier 97(1990), 3, Seite 597-600 (DE-627)NLEJ177069775 (DE-600)1481604-0 0305-0491 nnns volume:97 year:1990 number:3 pages:597-600 http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1990 3 597-600 |
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(DE-627)NLEJ187204403 (DE-599)GBVNLZ187204403 DE-627 ger DE-627 rakwb eng Circannual variations in mevalonate utilization in frog (Rana esculenta) 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bruscalupi, G. oth Castellano, F. oth Trentalance, A. oth in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Amsterdam : Elsevier 97(1990), 3, Seite 597-600 (DE-627)NLEJ177069775 (DE-600)1481604-0 0305-0491 nnns volume:97 year:1990 number:3 pages:597-600 http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1990 3 597-600 |
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(DE-627)NLEJ187204403 (DE-599)GBVNLZ187204403 DE-627 ger DE-627 rakwb eng Circannual variations in mevalonate utilization in frog (Rana esculenta) 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bruscalupi, G. oth Castellano, F. oth Trentalance, A. oth in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Amsterdam : Elsevier 97(1990), 3, Seite 597-600 (DE-627)NLEJ177069775 (DE-600)1481604-0 0305-0491 nnns volume:97 year:1990 number:3 pages:597-600 http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1990 3 597-600 |
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(DE-627)NLEJ187204403 (DE-599)GBVNLZ187204403 DE-627 ger DE-627 rakwb eng Circannual variations in mevalonate utilization in frog (Rana esculenta) 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bruscalupi, G. oth Castellano, F. oth Trentalance, A. oth in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Amsterdam : Elsevier 97(1990), 3, Seite 597-600 (DE-627)NLEJ177069775 (DE-600)1481604-0 0305-0491 nnns volume:97 year:1990 number:3 pages:597-600 http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1990 3 597-600 |
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(DE-627)NLEJ187204403 (DE-599)GBVNLZ187204403 DE-627 ger DE-627 rakwb eng Circannual variations in mevalonate utilization in frog (Rana esculenta) 1990 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bruscalupi, G. oth Castellano, F. oth Trentalance, A. oth in Comparative Biochemistry and Physiology -- Part B: Biochemistry and Amsterdam : Elsevier 97(1990), 3, Seite 597-600 (DE-627)NLEJ177069775 (DE-600)1481604-0 0305-0491 nnns volume:97 year:1990 number:3 pages:597-600 http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 97 1990 3 597-600 |
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Circannual variations in mevalonate utilization in frog (Rana esculenta) |
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1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. |
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1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. |
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1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation. |
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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">NLEJ187204403</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707070713.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1990 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ187204403</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ187204403</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">Circannual variations in mevalonate utilization in frog (Rana esculenta)</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1990</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">1. The fate of mevalonate, the product of HMGCoA reductase, was studied in male and female frogs (Rana esculenta) in order to explain the circannual variations of enzyme activity.2. The incorporation of 2-^1^4C MVA into unsaponifiable lipids, cholesterol and dolichol in liver, plasma and eggs was followed.3. Labeled MVA shows a different utilization depending on season and sex. In spring and summer cholesterol synthesis is related to hepatic reserve storage in both sexes, while the peak of enzyme activity, present only in females in fall, seems committed to cholesterol export into the blood and uptake by the oocytes.4. The presence of a MVA-derived protein identifiable with vitellogenin and labeled on the lipid moiety, suggests that HMGCoA reductase activity in fall is committed to the lipidation of this protein essential for oocyte maturation.</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">Bruscalupi, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Castellano, F.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Trentalance, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Comparative Biochemistry and Physiology -- Part B: Biochemistry and</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">97(1990), 3, Seite 597-600</subfield><subfield code="w">(DE-627)NLEJ177069775</subfield><subfield code="w">(DE-600)1481604-0</subfield><subfield code="x">0305-0491</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:97</subfield><subfield code="g">year:1990</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:597-600</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0305-0491(90)90165-P</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">97</subfield><subfield code="j">1990</subfield><subfield code="e">3</subfield><subfield code="h">597-600</subfield></datafield></record></collection>
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7.401434 |