Studies on human triosephosphate isomerase
A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1971 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 146(1971), 1, Seite 312-320 |
| Übergeordnetes Werk: |
volume:146 ; year:1971 ; number:1 ; pages:312-320 |
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| 520 | |a A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. | ||
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| 700 | 1 | |a Rozacky, E.E. |4 oth | |
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| 700 | 1 | |a Barton, R.A. |4 oth | |
| 700 | 1 | |a Gracy, R.W. |4 oth | |
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(DE-627)NLEJ184801982 (DE-599)GBVNLZ184801982 DE-627 ger DE-627 rakwb eng Studies on human triosephosphate isomerase 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rozacky, E.E. oth Sawyer, T.H. oth Barton, R.A. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 146(1971), 1, Seite 312-320 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:146 year:1971 number:1 pages:312-320 http://dx.doi.org/10.1016/S0003-9861(71)80069-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 146 1971 1 312-320 |
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(DE-627)NLEJ184801982 (DE-599)GBVNLZ184801982 DE-627 ger DE-627 rakwb eng Studies on human triosephosphate isomerase 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rozacky, E.E. oth Sawyer, T.H. oth Barton, R.A. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 146(1971), 1, Seite 312-320 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:146 year:1971 number:1 pages:312-320 http://dx.doi.org/10.1016/S0003-9861(71)80069-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 146 1971 1 312-320 |
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(DE-627)NLEJ184801982 (DE-599)GBVNLZ184801982 DE-627 ger DE-627 rakwb eng Studies on human triosephosphate isomerase 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rozacky, E.E. oth Sawyer, T.H. oth Barton, R.A. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 146(1971), 1, Seite 312-320 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:146 year:1971 number:1 pages:312-320 http://dx.doi.org/10.1016/S0003-9861(71)80069-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 146 1971 1 312-320 |
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(DE-627)NLEJ184801982 (DE-599)GBVNLZ184801982 DE-627 ger DE-627 rakwb eng Studies on human triosephosphate isomerase 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rozacky, E.E. oth Sawyer, T.H. oth Barton, R.A. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 146(1971), 1, Seite 312-320 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:146 year:1971 number:1 pages:312-320 http://dx.doi.org/10.1016/S0003-9861(71)80069-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 146 1971 1 312-320 |
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(DE-627)NLEJ184801982 (DE-599)GBVNLZ184801982 DE-627 ger DE-627 rakwb eng Studies on human triosephosphate isomerase 1971 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Rozacky, E.E. oth Sawyer, T.H. oth Barton, R.A. oth Gracy, R.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 146(1971), 1, Seite 312-320 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:146 year:1971 number:1 pages:312-320 http://dx.doi.org/10.1016/S0003-9861(71)80069-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 146 1971 1 312-320 |
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A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. |
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A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. |
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A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed. |
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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">NLEJ184801982</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707001044.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1971 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ184801982</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ184801982</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">Studies on human triosephosphate isomerase</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1971</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">A procedure for the isolation of crystalline triosephosphate isomerase from human erythrocytes is described. The isolated enzyme, after a 4500-fold purification has a specific activity of approximately 8000 μmoles of d-glyceraldehyde 3-phosphate converted to dihydroxyacetone phosphate per minute per milligram. The enzyme is judged to be homogeneous by the criteria of analytical ultracentrifugation, zone electrophoresis, and rechromatography. Molecular weight determinations by sedimentation equilibrium ultracentrifugation and gel filtration yield a value of 56,000 daltons. The amino acid composition of the enzyme has also been established. The enzyme from human erythrocytes has been resolved into three catalytically active components by isoelectric focusing. The major peak containing 76% of the triosephosphate isomerase activity has an isoelectric pH of 6.0. The two minor peaks with isoelectric pH values of 5.5 and 6.4 contain 22 and 2% of the enzyme activity, respectively. Several possible explanations for this multiplicity are discussed.</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">Rozacky, E.E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sawyer, T.H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Barton, R.A.</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">146(1971), 1, Seite 312-320</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:146</subfield><subfield code="g">year:1971</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:312-320</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/S0003-9861(71)80069-3</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">146</subfield><subfield code="j">1971</subfield><subfield code="e">1</subfield><subfield code="h">312-320</subfield></datafield></record></collection>
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7.400032 |