The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues
Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative...
Ausführliche Beschreibung
Gespeichert 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 |
|---|---|
| Übergeordnetes Werk: |
in: FEBS Letters - Amsterdam : Elsevier, 314(1992), 3, Seite 419-424 |
| Übergeordnetes Werk: |
volume:314 ; year:1992 ; number:3 ; pages:419-424 |
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| 245 | 1 | 4 | |a The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues |
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| 520 | |a Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. | ||
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(DE-627)NLEJ173439527 (DE-599)GBVNLZ173439527 DE-627 ger DE-627 rakwb eng The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Newbold, R.J. oth Hewson, R. oth Whitford, D. oth in FEBS Letters Amsterdam : Elsevier 314(1992), 3, Seite 419-424 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:314 year:1992 number:3 pages:419-424 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 314 1992 3 419-424 |
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(DE-627)NLEJ173439527 (DE-599)GBVNLZ173439527 DE-627 ger DE-627 rakwb eng The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Newbold, R.J. oth Hewson, R. oth Whitford, D. oth in FEBS Letters Amsterdam : Elsevier 314(1992), 3, Seite 419-424 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:314 year:1992 number:3 pages:419-424 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 314 1992 3 419-424 |
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(DE-627)NLEJ173439527 (DE-599)GBVNLZ173439527 DE-627 ger DE-627 rakwb eng The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Newbold, R.J. oth Hewson, R. oth Whitford, D. oth in FEBS Letters Amsterdam : Elsevier 314(1992), 3, Seite 419-424 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:314 year:1992 number:3 pages:419-424 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 314 1992 3 419-424 |
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(DE-627)NLEJ173439527 (DE-599)GBVNLZ173439527 DE-627 ger DE-627 rakwb eng The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Newbold, R.J. oth Hewson, R. oth Whitford, D. oth in FEBS Letters Amsterdam : Elsevier 314(1992), 3, Seite 419-424 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:314 year:1992 number:3 pages:419-424 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 314 1992 3 419-424 |
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(DE-627)NLEJ173439527 (DE-599)GBVNLZ173439527 DE-627 ger DE-627 rakwb eng The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Newbold, R.J. oth Hewson, R. oth Whitford, D. oth in FEBS Letters Amsterdam : Elsevier 314(1992), 3, Seite 419-424 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:314 year:1992 number:3 pages:419-424 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 314 1992 3 419-424 |
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thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues |
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The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues |
| abstract |
Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. |
| abstractGer |
Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. |
| abstract_unstemmed |
Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein. |
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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">NLEJ173439527</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705185644.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1992 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ173439527</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ173439527</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="4"><subfield code="a">The thermal stability of the tryptic fragment of bovine microsomal cytochrome b"5 and a variant containing six additional residues</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">Thermally induced denaturation has been measured for both oxidised and reduced forms of the tryptic fragment or bovine microsomal cytochrome b"5 using spectrophotometric methods. In the oxidised state, the tryptic fragment of cytochrome b"5 (Ala^7-Lys^9^0) denatures in a single cooperative transition with a midpoint temperature (T"m) of ~ 67^oC (pH 7.0). The reduced form of the tryptic fragment of cytochrome b"5 shows a higher transition temperature of ~ 73^oC at pH 7.0 and this is reflected in the values of ΔH"m, ΔS"m, and Δ(ΔG) of ~ 310kJ . mol^-^1, 900J . mol^-^1 . K^-^1 and 5 kJ . mol^-^1. Increased thermal stability is demonstrated for a variant protein that contains the first 90 amino acid residues of cytochrome b"5. These novel increases in stability are observed in both redox states and result from the presence of six additional residues at the amino-terminus. The two forms of cytochrome b"5 do not differ significantly in structure with the results suggesting that the reorganisation energy (λ) of the variant protein, as measured indirectly from redox-linked differences in conformational stability, is small. Consequently the reported subtle differences in reactivity between variants of cytochrome b"5 may result from the presence of additional N-terminal residues on the surface of the protein.</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">Newbold, R.J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hewson, R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Whitford, D.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">FEBS Letters</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">314(1992), 3, Seite 419-424</subfield><subfield code="w">(DE-627)NLEJ173141048</subfield><subfield code="w">(DE-600)1460391-3</subfield><subfield code="x">0014-5793</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:314</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:419-424</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0014-5793(92)81518-Q</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">314</subfield><subfield code="j">1992</subfield><subfield code="e">3</subfield><subfield code="h">419-424</subfield></datafield></record></collection>
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7.399008 |