Purification and characterization of a protein kinase modulator from rat mammary gland
A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole,...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1977 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA - Enzymology - Amsterdam : Elsevier, 483(1977), 2, Seite 279-293 |
| Übergeordnetes Werk: |
volume:483 ; year:1977 ; number:2 ; pages:279-293 |
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| 245 | 1 | 0 | |a Purification and characterization of a protein kinase modulator from rat mammary gland |
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| 520 | |a A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. | ||
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(DE-627)NLEJ185763308 (DE-599)GBVNLZ185763308 DE-627 ger DE-627 rakwb eng Purification and characterization of a protein kinase modulator from rat mammary gland 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Majumder, G.C. oth in BBA - Enzymology Amsterdam : Elsevier 483(1977), 2, Seite 279-293 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:483 year:1977 number:2 pages:279-293 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 483 1977 2 279-293 |
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(DE-627)NLEJ185763308 (DE-599)GBVNLZ185763308 DE-627 ger DE-627 rakwb eng Purification and characterization of a protein kinase modulator from rat mammary gland 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Majumder, G.C. oth in BBA - Enzymology Amsterdam : Elsevier 483(1977), 2, Seite 279-293 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:483 year:1977 number:2 pages:279-293 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 483 1977 2 279-293 |
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(DE-627)NLEJ185763308 (DE-599)GBVNLZ185763308 DE-627 ger DE-627 rakwb eng Purification and characterization of a protein kinase modulator from rat mammary gland 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Majumder, G.C. oth in BBA - Enzymology Amsterdam : Elsevier 483(1977), 2, Seite 279-293 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:483 year:1977 number:2 pages:279-293 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 483 1977 2 279-293 |
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(DE-627)NLEJ185763308 (DE-599)GBVNLZ185763308 DE-627 ger DE-627 rakwb eng Purification and characterization of a protein kinase modulator from rat mammary gland 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Majumder, G.C. oth in BBA - Enzymology Amsterdam : Elsevier 483(1977), 2, Seite 279-293 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:483 year:1977 number:2 pages:279-293 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 483 1977 2 279-293 |
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(DE-627)NLEJ185763308 (DE-599)GBVNLZ185763308 DE-627 ger DE-627 rakwb eng Purification and characterization of a protein kinase modulator from rat mammary gland 1977 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Majumder, G.C. oth in BBA - Enzymology Amsterdam : Elsevier 483(1977), 2, Seite 279-293 (DE-627)NLEJ185751202 (DE-600)2209533-0 0005-2744 nnns volume:483 year:1977 number:2 pages:279-293 http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 483 1977 2 279-293 |
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Purification and characterization of a protein kinase modulator from rat mammary gland |
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A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. |
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A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. |
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A factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity. |
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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">NLEJ185763308</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707024929.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1977 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ185763308</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ185763308</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">Purification and characterization of a protein kinase modulator from rat mammary gland</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1977</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 factor (Modulator II) partially purified from lactating rat mammary gland causes a marked substrate-dependent inhibition of the activity of mammary cytosol cyclic AMP-dependent protein kinase (ATP : protamine O-phosphotransferase, EC 2.7.1.70) for the phosphorylation of casein, calf thymus whole, F-1, F-2b, F-3 and F-2a histones and mammary whole histones and mitochondrial, plasma membrane and ribosomal phosphoproteins whereas it has no effect on the phosphorylation of protamine. Modulator II is stable to heating at 100^oC for 30 min, is assumed to be a protein since it is inactivated by treatment with trypsin and it has a molecular weight of approximately 18 000 by gel exclusion. The modulator acts noncompetitively with respect to protein kinase substrates, ATP and histones and to activator molecules, cyclic AMP and Co^2^+. The modulator does not function by destroying ATP nor by acting as a phosphoprotein phosphatase. However, it causes a marked alteration in the pH and metal ion activation properties of the kinase. The reactivities of the modulator were nearly identical with the holoenzyme and the catalytic subunit of protein kinase. The results suggest that the modulator (M) interacts directly with the catalytic subunit (C) of cyclic AMP-dependent protein kinase to cause the formation of a complex (CM) which has an altered pattern of substrate specificity.</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">Majumder, G.C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">BBA - Enzymology</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">483(1977), 2, Seite 279-293</subfield><subfield code="w">(DE-627)NLEJ185751202</subfield><subfield code="w">(DE-600)2209533-0</subfield><subfield code="x">0005-2744</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:483</subfield><subfield code="g">year:1977</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:279-293</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0005-2744(77)90056-0</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">483</subfield><subfield code="j">1977</subfield><subfield code="e">2</subfield><subfield code="h">279-293</subfield></datafield></record></collection>
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7.3983173 |