Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis
Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more ba...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1973 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 157(1973), 2, Seite 580-587 |
| Übergeordnetes Werk: |
volume:157 ; year:1973 ; number:2 ; pages:580-587 |
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NLEJ183390784 |
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| 520 | |a Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. | ||
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(DE-627)NLEJ183390784 (DE-599)GBVNLZ183390784 DE-627 ger DE-627 rakwb eng Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mo, Y. oth Harris, B.G. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 157(1973), 2, Seite 580-587 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:157 year:1973 number:2 pages:580-587 http://dx.doi.org/10.1016/0003-9861(73)90677-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 157 1973 2 580-587 |
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(DE-627)NLEJ183390784 (DE-599)GBVNLZ183390784 DE-627 ger DE-627 rakwb eng Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mo, Y. oth Harris, B.G. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 157(1973), 2, Seite 580-587 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:157 year:1973 number:2 pages:580-587 http://dx.doi.org/10.1016/0003-9861(73)90677-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 157 1973 2 580-587 |
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(DE-627)NLEJ183390784 (DE-599)GBVNLZ183390784 DE-627 ger DE-627 rakwb eng Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mo, Y. oth Harris, B.G. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 157(1973), 2, Seite 580-587 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:157 year:1973 number:2 pages:580-587 http://dx.doi.org/10.1016/0003-9861(73)90677-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 157 1973 2 580-587 |
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(DE-627)NLEJ183390784 (DE-599)GBVNLZ183390784 DE-627 ger DE-627 rakwb eng Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mo, Y. oth Harris, B.G. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 157(1973), 2, Seite 580-587 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:157 year:1973 number:2 pages:580-587 http://dx.doi.org/10.1016/0003-9861(73)90677-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 157 1973 2 580-587 |
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(DE-627)NLEJ183390784 (DE-599)GBVNLZ183390784 DE-627 ger DE-627 rakwb eng Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Mo, Y. oth Harris, B.G. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 157(1973), 2, Seite 580-587 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:157 year:1973 number:2 pages:580-587 http://dx.doi.org/10.1016/0003-9861(73)90677-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 157 1973 2 580-587 |
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triosephosphate isomerases and aldolases from light- and dark-grown euglena gracilis |
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Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis |
| abstract |
Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. |
| abstractGer |
Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. |
| abstract_unstemmed |
Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase. |
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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">NLEJ183390784</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706201858.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1973 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183390784</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183390784</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">Triosephosphate isomerases and aldolases from light- and dark-grown Euglena gracilis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1973</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">Euglena gracilis synthesizes two distinct types of triosephosphate isomerase which can be resolved by isoelectric focusing. The more acidic Type A isomerase (pI = 4.4) predominates when cells are grown photoautotrophically and is localized in the chloroplasts. The Type B isoenzyme exhibits a more basic isoelectric pH (pI = 4.8), predominates under heterotrophic growth conditions and is of cytoplasmic origin. The two isoenzymes exhibit similar molecular weights (56,000-60,000) and catalytic properties but can be distinguished by their pH activity profiles. The situation parallels that of fructose diphosphate aldolase where a chloroplastic Class I enzyme (pI = 4.6, M"r 120,000) found in autotrophically grown cells can be resolved from the cytoplasmic Class II (pI = 5.7, M"r 88,000) enzyme which predominates under heterotrophic conditions. Inhibition of chloroplastic 70S ribosomal synthesis by chloramphenicol blocks the formation of the Type A triosephosphate isomerase and the Class I aldolase.</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">Mo, Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Harris, B.G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gracy, R.W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Archives of Biochemistry and Biophysics</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">157(1973), 2, Seite 580-587</subfield><subfield code="w">(DE-627)NLEJ177020539</subfield><subfield code="w">(DE-600)1461378-5</subfield><subfield code="x">0003-9861</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:157</subfield><subfield code="g">year:1973</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:580-587</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(73)90677-2</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">157</subfield><subfield code="j">1973</subfield><subfield code="e">2</subfield><subfield code="h">580-587</subfield></datafield></record></collection>
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