Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis
The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981)...
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1983 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular - Amsterdam : Elsevier, 748(1983), 2, Seite 213-219 |
| Übergeordnetes Werk: |
volume:748 ; year:1983 ; number:2 ; pages:213-219 |
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| 245 | 1 | 0 | |a Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis |
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| 520 | |a The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. | ||
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(DE-627)NLEJ186900775 (DE-599)GBVNLZ186900775 DE-627 ger DE-627 rakwb eng Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Brans, A.M.M. oth Hoekman, W.A. oth Slingsby, C. oth Bloemendal, H. oth De Jong, W.W. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 748(1983), 2, Seite 213-219 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:748 year:1983 number:2 pages:213-219 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 748 1983 2 213-219 |
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(DE-627)NLEJ186900775 (DE-599)GBVNLZ186900775 DE-627 ger DE-627 rakwb eng Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Brans, A.M.M. oth Hoekman, W.A. oth Slingsby, C. oth Bloemendal, H. oth De Jong, W.W. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 748(1983), 2, Seite 213-219 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:748 year:1983 number:2 pages:213-219 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 748 1983 2 213-219 |
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(DE-627)NLEJ186900775 (DE-599)GBVNLZ186900775 DE-627 ger DE-627 rakwb eng Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Brans, A.M.M. oth Hoekman, W.A. oth Slingsby, C. oth Bloemendal, H. oth De Jong, W.W. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 748(1983), 2, Seite 213-219 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:748 year:1983 number:2 pages:213-219 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 748 1983 2 213-219 |
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(DE-627)NLEJ186900775 (DE-599)GBVNLZ186900775 DE-627 ger DE-627 rakwb eng Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Brans, A.M.M. oth Hoekman, W.A. oth Slingsby, C. oth Bloemendal, H. oth De Jong, W.W. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 748(1983), 2, Seite 213-219 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:748 year:1983 number:2 pages:213-219 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 748 1983 2 213-219 |
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(DE-627)NLEJ186900775 (DE-599)GBVNLZ186900775 DE-627 ger DE-627 rakwb eng Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis 1983 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Berbers, G.A.M. oth Brans, A.M.M. oth Hoekman, W.A. oth Slingsby, C. oth Bloemendal, H. oth De Jong, W.W. oth in Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Amsterdam : Elsevier 748(1983), 2, Seite 213-219 (DE-627)NLEJ185338283 (DE-600)2209539-1 0167-4838 nnns volume:748 year:1983 number:2 pages:213-219 http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 748 1983 2 213-219 |
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aggregation behavior of the bovine β-crystallin b"p chain studied by limited proteolysis |
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Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis |
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The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. |
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The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. |
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The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p. |
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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">NLEJ186900775</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707062251.0</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)NLEJ186900775</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186900775</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">Aggregation behavior of the bovine β-crystallin B"p chain studied by limited proteolysis</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">The bovine β-crystallin B"p chain is organized into two very similar domains, with short extensions at both N- and C-termini, and two alternative models for the βB"p dimer have been proposed (Wistow, G., Slingsby, C., Blundell, T., Driessen, H.P.C., De Jong, W.W. And Bloemendal, H. (1981) FEBS Lett. 133, 9-16). By limited proteolysis the C-terminal arms can be cleaved off rapidly from the βB"p dimer, while the N-terminal arms are more difficult to remove. Trypsin divides the βB"p chain into two fragments which approximately correspond to the two structural domains. Dissociation and reassociation of the different products of limited proteolysis indicated that: the C-terminal arm extends freely from the surface and is not involved in subunit-contact; at least one N-terminal arms seems required for dimer formation; the N-terminal domains have a greater tendency to associate than the C-terminal domains and, when mixed, the purified domains reassociate partially to a M"r 50 000 structure like native βB"p. These findings support the more extended dimer model of βB"p.</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">Berbers, G.A.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Brans, A.M.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hoekman, W.A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Slingsby, C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Bloemendal, H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">De Jong, W.W.</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">748(1983), 2, Seite 213-219</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:748</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:213-219</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90297-2</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">748</subfield><subfield code="j">1983</subfield><subfield code="e">2</subfield><subfield code="h">213-219</subfield></datafield></record></collection>
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