Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor
An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel pe...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1992 |
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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, 297(1992), 2, Seite 296-303 |
| Übergeordnetes Werk: |
volume:297 ; year:1992 ; number:2 ; pages:296-303 |
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| 245 | 1 | 0 | |a Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor |
| 264 | 1 | |c 1992 | |
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| 520 | |a An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. | ||
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(DE-627)NLEJ183429516 (DE-599)GBVNLZ183429516 DE-627 ger DE-627 rakwb eng Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hoffmann, R. oth Jung, S. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 297(1992), 2, Seite 296-303 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:297 year:1992 number:2 pages:296-303 http://dx.doi.org/10.1016/0003-9861(92)90676-N GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 297 1992 2 296-303 |
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(DE-627)NLEJ183429516 (DE-599)GBVNLZ183429516 DE-627 ger DE-627 rakwb eng Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hoffmann, R. oth Jung, S. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 297(1992), 2, Seite 296-303 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:297 year:1992 number:2 pages:296-303 http://dx.doi.org/10.1016/0003-9861(92)90676-N GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 297 1992 2 296-303 |
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(DE-627)NLEJ183429516 (DE-599)GBVNLZ183429516 DE-627 ger DE-627 rakwb eng Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hoffmann, R. oth Jung, S. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 297(1992), 2, Seite 296-303 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:297 year:1992 number:2 pages:296-303 http://dx.doi.org/10.1016/0003-9861(92)90676-N GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 297 1992 2 296-303 |
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(DE-627)NLEJ183429516 (DE-599)GBVNLZ183429516 DE-627 ger DE-627 rakwb eng Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hoffmann, R. oth Jung, S. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 297(1992), 2, Seite 296-303 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:297 year:1992 number:2 pages:296-303 http://dx.doi.org/10.1016/0003-9861(92)90676-N GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 297 1992 2 296-303 |
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(DE-627)NLEJ183429516 (DE-599)GBVNLZ183429516 DE-627 ger DE-627 rakwb eng Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hoffmann, R. oth Jung, S. oth Hofer, H.W. oth in Archives of Biochemistry and Biophysics Amsterdam : Elsevier 297(1992), 2, Seite 296-303 (DE-627)NLEJ177020539 (DE-600)1461378-5 0003-9861 nnns volume:297 year:1992 number:2 pages:296-303 http://dx.doi.org/10.1016/0003-9861(92)90676-N GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 297 1992 2 296-303 |
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Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor |
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association of a heat-stable inhibitor protein with cyclic-3',5'-amp-dependent protein kinase from the nematode ascaris suum: purification and characterization of the inhibitor |
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Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor |
| abstract |
An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. |
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An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. |
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An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode. |
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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">NLEJ183429516</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706202526.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1992 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ183429516</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ183429516</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">Association of a heat-stable inhibitor protein with cyclic-3',5'-AMP-dependent protein kinase from the nematode Ascaris suum: Purification and characterization of the inhibitor</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1992</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">An inhibitor protein of the catalytic subunit of the cyclic 3',5'-AMP-dependent protein kinase from the nematode Ascaris suum was isolated and characterized. The molecular weight of the inhibitor was estimated as 28,000 by electrophoresis under denaturing conditions and as 30,000 by gel permeation chromatography on Superose 12. The trypsin-labile inhibitor was resistant to short incubations (=< 5 min) at temperatures up to 95 ^oC and at pH 3. It affected the protein kinase from Ascaris and bovine heart with almost the same affinity, and inhibition was not relieved by the presence of cAMP and cGMP. However, the inhibition was antagonized by low concentrations of heparin. Unlike in mammalian tissues, the concentration of the inhibitor was sufficiently high to exert at least 90% inhibition of the protein kinase activity in Ascaris muscle. Therefore, the inhibitor may play a role in cellular regulation in the nematode.</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">Hoffmann, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jung, S.</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">297(1992), 2, Seite 296-303</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:297</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:296-303</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1016/0003-9861(92)90676-N</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">297</subfield><subfield code="j">1992</subfield><subfield code="e">2</subfield><subfield code="h">296-303</subfield></datafield></record></collection>
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