Phosphofructokinase from mollusc muscle is activated by phosphorylation
Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphor...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1991 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Archives of Biochemistry and Biophysics - Amsterdam : Elsevier, 287(1991), 2, Seite 263-267 |
| Übergeordnetes Werk: |
volume:287 ; year:1991 ; number:2 ; pages:263-267 |
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NLEJ183440315 |
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| 245 | 1 | 0 | |a Phosphofructokinase from mollusc muscle is activated by phosphorylation |
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| 520 | |a Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. | ||
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(DE-627)NLEJ183440315 (DE-599)GBVNLZ183440315 DE-627 ger DE-627 rakwb eng Phosphofructokinase from mollusc muscle is activated by phosphorylation 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Biethinger, M. oth Hoffmann, R. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 287(1991), 2, Seite 263-267 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:287 year:1991 number:2 pages:263-267 http://dx.doi.org/10.1016/0003-9861(91)90477-Z GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 287 1991 2 263-267 |
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(DE-627)NLEJ183440315 (DE-599)GBVNLZ183440315 DE-627 ger DE-627 rakwb eng Phosphofructokinase from mollusc muscle is activated by phosphorylation 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Biethinger, M. oth Hoffmann, R. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 287(1991), 2, Seite 263-267 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:287 year:1991 number:2 pages:263-267 http://dx.doi.org/10.1016/0003-9861(91)90477-Z GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 287 1991 2 263-267 |
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(DE-627)NLEJ183440315 (DE-599)GBVNLZ183440315 DE-627 ger DE-627 rakwb eng Phosphofructokinase from mollusc muscle is activated by phosphorylation 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Biethinger, M. oth Hoffmann, R. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 287(1991), 2, Seite 263-267 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:287 year:1991 number:2 pages:263-267 http://dx.doi.org/10.1016/0003-9861(91)90477-Z GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 287 1991 2 263-267 |
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(DE-627)NLEJ183440315 (DE-599)GBVNLZ183440315 DE-627 ger DE-627 rakwb eng Phosphofructokinase from mollusc muscle is activated by phosphorylation 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Biethinger, M. oth Hoffmann, R. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 287(1991), 2, Seite 263-267 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:287 year:1991 number:2 pages:263-267 http://dx.doi.org/10.1016/0003-9861(91)90477-Z GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 287 1991 2 263-267 |
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(DE-627)NLEJ183440315 (DE-599)GBVNLZ183440315 DE-627 ger DE-627 rakwb eng Phosphofructokinase from mollusc muscle is activated by phosphorylation 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Biethinger, M. oth Hoffmann, R. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 287(1991), 2, Seite 263-267 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:287 year:1991 number:2 pages:263-267 http://dx.doi.org/10.1016/0003-9861(91)90477-Z GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 287 1991 2 263-267 |
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Phosphofructokinase from mollusc muscle is activated by phosphorylation |
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Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. |
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Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. |
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Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate. |
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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">NLEJ183440315</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706202714.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1991 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183440315</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183440315</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">Phosphofructokinase from mollusc muscle is activated by phosphorylation</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1991</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">Phosphofructokinase was purified from muscle tissue of two different molluscs, edible snails, Helix pomatia (gastropoda), and mussels, Mytilus edulis (bivalvia). Under denaturing conditions, both enzymes had a molecular mass of 82 kDa. In the presence of ATP-Mg^2^+, the enzymes were rapidly phosphorylated in vitro by the catalytic subunit of cyclic AMP (cAMP)-dependent protein kinase purified from snail muscle and also by the C subunit of protein kinase from bovine heart. The extent of phosphorylation was 0.6 and 0.5 phosphate residues per subunit for the snail and the mussel phosphofructokinase, respectively. Phosphorylation of both phosphofructokinases effected a decrease in ATP inhibition at neutral or slightly acidic pH values and increased the affinity for fructose 6-phosphate. The resulting activation in the presence of suboptimum fructose 6-phosphate concentrations was more distinct for the snail enzyme. In addition, phosphorylated phosphofructokinase from mussels exhibited a marked increase in V"m"a"x when activated by either 5'-AMP or fructose 2,6-bisphosphate.</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">Biethinger, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hoffmann, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hofer, H.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">287(1991), 2, Seite 263-267</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:287</subfield><subfield code="g">year:1991</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:263-267</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(91)90477-Z</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">287</subfield><subfield code="j">1991</subfield><subfield code="e">2</subfield><subfield code="h">263-267</subfield></datafield></record></collection>
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