Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus
Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonom...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1981 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 661(1981), 1, Seite 158-163 |
| Übergeordnetes Werk: |
volume:661 ; year:1981 ; number:1 ; pages:158-163 |
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| 520 | |a Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. | ||
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(DE-627)NLEJ185759556 (DE-599)GBVNLZ185759556 DE-627 ger DE-627 rakwb eng Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Simon, W.A. oth Hofer, H.W. oth in BBA - Enzymology Amsterdam : Elsevier 661(1981), 1, Seite 158-163 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:661 year:1981 number:1 pages:158-163 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(81)90095-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 661 1981 1 158-163 |
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(DE-627)NLEJ185759556 (DE-599)GBVNLZ185759556 DE-627 ger DE-627 rakwb eng Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Simon, W.A. oth Hofer, H.W. oth in BBA - Enzymology Amsterdam : Elsevier 661(1981), 1, Seite 158-163 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:661 year:1981 number:1 pages:158-163 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(81)90095-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 661 1981 1 158-163 |
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(DE-627)NLEJ185759556 (DE-599)GBVNLZ185759556 DE-627 ger DE-627 rakwb eng Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Simon, W.A. oth Hofer, H.W. oth in BBA - Enzymology Amsterdam : Elsevier 661(1981), 1, Seite 158-163 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:661 year:1981 number:1 pages:158-163 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(81)90095-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 661 1981 1 158-163 |
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(DE-627)NLEJ185759556 (DE-599)GBVNLZ185759556 DE-627 ger DE-627 rakwb eng Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Simon, W.A. oth Hofer, H.W. oth in BBA - Enzymology Amsterdam : Elsevier 661(1981), 1, Seite 158-163 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:661 year:1981 number:1 pages:158-163 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(81)90095-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 661 1981 1 158-163 |
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(DE-627)NLEJ185759556 (DE-599)GBVNLZ185759556 DE-627 ger DE-627 rakwb eng Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus 1981 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Simon, W.A. oth Hofer, H.W. oth in BBA - Enzymology Amsterdam : Elsevier 661(1981), 1, Seite 158-163 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:661 year:1981 number:1 pages:158-163 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(81)90095-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 661 1981 1 158-163 |
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Phosphofructokinases from Lactobacteriaceae - II. Purification and properties of phosphofructokinase from Streptococcus thermophilus |
| abstract |
Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. |
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Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. |
| abstract_unstemmed |
Phosphofructokinase (ATP : d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from Streptococcus thermophilus has been purified. It is a tetramer composed of identical subunits of molecular weight 36 000 and exhibits Michaelis-Menten kinetics. Compared to the phosphofructokinases from taxonomically related bacteria, the enzyme from S. thermophilus is more stable at high temperatures. In addition, it has been demonstrated that the phosphofructokinases from lactobacteria and also from Bacillus stearothermophilus show immunologic cross-reaction. In spite of the significantly different kinetic properties and the different thermostability of these enzymes, this finding indicates great structural resemblance. |
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