Preparation of native α and β subunits from canine hemoglobin
Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobin...
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Englisch |
| Erschienen: |
1983 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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in: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular - Amsterdam : Elsevier, 744(1983), 1, Seite 71-75 |
| Übergeordnetes Werk: |
volume:744 ; year:1983 ; number:1 ; pages:71-75 |
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| 520 | |a Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. | ||
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(DE-627)NLEJ18690147X (DE-599)GBVNLZ18690147X DE-627 ger DE-627 rakwb eng Preparation of native α and β subunits from canine hemoglobin 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Enoki, Y. oth Ochiai, T. oth Ohga, Y. oth Kohzuki, H. oth Sakata, S. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 744(1983), 1, Seite 71-75 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:744 year:1983 number:1 pages:71-75 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 744 1983 1 71-75 |
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(DE-627)NLEJ18690147X (DE-599)GBVNLZ18690147X DE-627 ger DE-627 rakwb eng Preparation of native α and β subunits from canine hemoglobin 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Enoki, Y. oth Ochiai, T. oth Ohga, Y. oth Kohzuki, H. oth Sakata, S. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 744(1983), 1, Seite 71-75 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:744 year:1983 number:1 pages:71-75 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 744 1983 1 71-75 |
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(DE-627)NLEJ18690147X (DE-599)GBVNLZ18690147X DE-627 ger DE-627 rakwb eng Preparation of native α and β subunits from canine hemoglobin 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Enoki, Y. oth Ochiai, T. oth Ohga, Y. oth Kohzuki, H. oth Sakata, S. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 744(1983), 1, Seite 71-75 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:744 year:1983 number:1 pages:71-75 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 744 1983 1 71-75 |
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(DE-627)NLEJ18690147X (DE-599)GBVNLZ18690147X DE-627 ger DE-627 rakwb eng Preparation of native α and β subunits from canine hemoglobin 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Enoki, Y. oth Ochiai, T. oth Ohga, Y. oth Kohzuki, H. oth Sakata, S. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 744(1983), 1, Seite 71-75 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:744 year:1983 number:1 pages:71-75 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 744 1983 1 71-75 |
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(DE-627)NLEJ18690147X (DE-599)GBVNLZ18690147X DE-627 ger DE-627 rakwb eng Preparation of native α and β subunits from canine hemoglobin 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Enoki, Y. oth Ochiai, T. oth Ohga, Y. oth Kohzuki, H. oth Sakata, S. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 744(1983), 1, Seite 71-75 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:744 year:1983 number:1 pages:71-75 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 744 1983 1 71-75 |
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preparation of native α and β subunits from canine hemoglobin |
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Preparation of native α and β subunits from canine hemoglobin |
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Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. |
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Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. |
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Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form. |
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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">NLEJ18690147X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707062258.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1983 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ18690147X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ18690147X</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">Preparation of native α and β subunits from canine hemoglobin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1983</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">Preparation of native α and β subunits from non-primate hemoglobins has never been successful using the procedure of Bucci, E. and Fronticelli, C. ((1965 J. Biol. Chem. 240, PC551-552). We describe a method for isolating the constituent subunits from canine hemoglobin. Human-canine hybrid hemoglobins (α"2^C^a^nβ"2^A and α"2^Aβ"2^C^a^n) were prepared by acid hybridization techniques and DEAE-Sephadex chromatography. The hybrids were then reacted with an excess of p-chloromercuribenzoate under slightly acid conditions and the resultant α^C^a^n and β^C^a^n subunits were isolated by either anion- or cation-exchange chromatography. Identifications of the subunits were made by gel electrophoresis and amino acid analysis. After removal of the bound mercurials with β-mercaptoethanol, both subunits exhibited two reactive sulfhydryl groups per chain and were found to be fully in the native form, as judged by spectroscopy. By ultracentrifugal analysis, the α subunit was shown to be in a dimer-monomer equilibrium while the β subunit was largely in a tetrameric form.</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">Enoki, Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ochiai, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Ohga, Y.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kohzuki, H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sakata, S.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">744(1983), 1, Seite 71-75</subfield><subfield code="w">(DE-627)NLEJ185338283</subfield><subfield code="w">(DE-600)2209539-1</subfield><subfield code="x">0167-4838</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:744</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:71-75</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90342-4</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">744</subfield><subfield code="j">1983</subfield><subfield code="e">1</subfield><subfield code="h">71-75</subfield></datafield></record></collection>
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