Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry
A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers control...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Tetrahedron - Amsterdam : Elsevier, 49(1993), 36, Seite 7985-7996 |
| Übergeordnetes Werk: |
volume:49 ; year:1993 ; number:36 ; pages:7985-7996 |
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| 520 | |a A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. | ||
| 520 | |a A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. | ||
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| 700 | 1 | |a Tsarbopoulos, A. |4 oth | |
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| 700 | 1 | |a Liberles, S. |4 oth | |
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(DE-627)NLEJ175910499 (DE-599)GBVNLZ175910499 DE-627 ger DE-627 rakwb eng Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ganguly, A.K. oth Pramanik, B.N. oth Huang, E.C. oth Tsarbopoulos, A. oth Girijavallabhan, V.M. oth Liberles, S. oth in Tetrahedron Amsterdam : Elsevier 49(1993), 36, Seite 7985-7996 (DE-627)NLEJ175783357 (DE-600)2007072-X 0040-4020 nnns volume:49 year:1993 number:36 pages:7985-7996 http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1993 36 7985-7996 |
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(DE-627)NLEJ175910499 (DE-599)GBVNLZ175910499 DE-627 ger DE-627 rakwb eng Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ganguly, A.K. oth Pramanik, B.N. oth Huang, E.C. oth Tsarbopoulos, A. oth Girijavallabhan, V.M. oth Liberles, S. oth in Tetrahedron Amsterdam : Elsevier 49(1993), 36, Seite 7985-7996 (DE-627)NLEJ175783357 (DE-600)2007072-X 0040-4020 nnns volume:49 year:1993 number:36 pages:7985-7996 http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1993 36 7985-7996 |
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(DE-627)NLEJ175910499 (DE-599)GBVNLZ175910499 DE-627 ger DE-627 rakwb eng Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ganguly, A.K. oth Pramanik, B.N. oth Huang, E.C. oth Tsarbopoulos, A. oth Girijavallabhan, V.M. oth Liberles, S. oth in Tetrahedron Amsterdam : Elsevier 49(1993), 36, Seite 7985-7996 (DE-627)NLEJ175783357 (DE-600)2007072-X 0040-4020 nnns volume:49 year:1993 number:36 pages:7985-7996 http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1993 36 7985-7996 |
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(DE-627)NLEJ175910499 (DE-599)GBVNLZ175910499 DE-627 ger DE-627 rakwb eng Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ganguly, A.K. oth Pramanik, B.N. oth Huang, E.C. oth Tsarbopoulos, A. oth Girijavallabhan, V.M. oth Liberles, S. oth in Tetrahedron Amsterdam : Elsevier 49(1993), 36, Seite 7985-7996 (DE-627)NLEJ175783357 (DE-600)2007072-X 0040-4020 nnns volume:49 year:1993 number:36 pages:7985-7996 http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1993 36 7985-7996 |
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(DE-627)NLEJ175910499 (DE-599)GBVNLZ175910499 DE-627 ger DE-627 rakwb eng Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ganguly, A.K. oth Pramanik, B.N. oth Huang, E.C. oth Tsarbopoulos, A. oth Girijavallabhan, V.M. oth Liberles, S. oth in Tetrahedron Amsterdam : Elsevier 49(1993), 36, Seite 7985-7996 (DE-627)NLEJ175783357 (DE-600)2007072-X 0040-4020 nnns volume:49 year:1993 number:36 pages:7985-7996 http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 49 1993 36 7985-7996 |
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Studies of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry |
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A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. |
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A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. |
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A novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content. A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively. |
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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">NLEJ175910499</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706011425.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1993 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ175910499</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ175910499</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 of the Ras-GDP and Ras-GTP noncovalent complexes by electrospray mass spectrometry</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1993</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 novel MS based methodology utilizing electrospray ionization is described for the detection of the noncovalent interaction between a host protein (ras) and its guest ligands (GDP and GTP). The ras proteins are regulatory guanine nucleotide binding proteins which serve as signal transducers controlling cell proliferation or differentiation. They can exist in two interconvertible states of GDP-bound (inactive form) and GTP-bound (active form). The presence of the noncovalent complexes of ras-GDP and ras-GTP, as well as the unbound apo-ras protein, in various sample solutions containing biological buffers were confirmed by the observed average molecular weights of 19295, 19374, and 18852 Da, respectively. The stability of the observed GDP-bound and GTP-bound complexes is a combined function of solution pH and organic modifier content.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">A MS-based methodology employing electrospray ionization is described for the detection of the noncovalent interaction between the ras protein and the nucleotide ligands GDP and GTP. The observed average molecular weights of 19295 and 19374 Da confirmed the presence of ras-GDP and ras-GTP, respectively.</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">Ganguly, A.K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pramanik, B.N.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Huang, E.C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Tsarbopoulos, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Girijavallabhan, V.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Liberles, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Tetrahedron</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">49(1993), 36, Seite 7985-7996</subfield><subfield code="w">(DE-627)NLEJ175783357</subfield><subfield code="w">(DE-600)2007072-X</subfield><subfield code="x">0040-4020</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:49</subfield><subfield code="g">year:1993</subfield><subfield code="g">number:36</subfield><subfield code="g">pages:7985-7996</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)88022-4</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">49</subfield><subfield code="j">1993</subfield><subfield code="e">36</subfield><subfield code="h">7985-7996</subfield></datafield></record></collection>
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