Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments
Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most...
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1986 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: FEBS Letters - Amsterdam : Elsevier, 208(1986), 2, Seite 435-438 |
| Übergeordnetes Werk: |
volume:208 ; year:1986 ; number:2 ; pages:435-438 |
| Links: |
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NLEJ173303943 |
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| 520 | |a Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. | ||
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| 700 | 1 | |a Pavlik, M. |4 oth | |
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(DE-627)NLEJ173303943 (DE-599)GBVNLZ173303943 DE-627 ger DE-627 rakwb eng Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moravek, L. oth Kuhnemund, O. oth Havlicek, J.V. oth Kopecky, P. oth Pavlik, M. oth in FEBS Letters Amsterdam : Elsevier 208(1986), 2, Seite 435-438 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:208 year:1986 number:2 pages:435-438 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 208 1986 2 435-438 |
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(DE-627)NLEJ173303943 (DE-599)GBVNLZ173303943 DE-627 ger DE-627 rakwb eng Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moravek, L. oth Kuhnemund, O. oth Havlicek, J.V. oth Kopecky, P. oth Pavlik, M. oth in FEBS Letters Amsterdam : Elsevier 208(1986), 2, Seite 435-438 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:208 year:1986 number:2 pages:435-438 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 208 1986 2 435-438 |
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(DE-627)NLEJ173303943 (DE-599)GBVNLZ173303943 DE-627 ger DE-627 rakwb eng Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moravek, L. oth Kuhnemund, O. oth Havlicek, J.V. oth Kopecky, P. oth Pavlik, M. oth in FEBS Letters Amsterdam : Elsevier 208(1986), 2, Seite 435-438 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:208 year:1986 number:2 pages:435-438 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 208 1986 2 435-438 |
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(DE-627)NLEJ173303943 (DE-599)GBVNLZ173303943 DE-627 ger DE-627 rakwb eng Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moravek, L. oth Kuhnemund, O. oth Havlicek, J.V. oth Kopecky, P. oth Pavlik, M. oth in FEBS Letters Amsterdam : Elsevier 208(1986), 2, Seite 435-438 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:208 year:1986 number:2 pages:435-438 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 208 1986 2 435-438 |
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(DE-627)NLEJ173303943 (DE-599)GBVNLZ173303943 DE-627 ger DE-627 rakwb eng Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments 1986 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Moravek, L. oth Kuhnemund, O. oth Havlicek, J.V. oth Kopecky, P. oth Pavlik, M. oth in FEBS Letters Amsterdam : Elsevier 208(1986), 2, Seite 435-438 (DE-627)NLEJ173141048 (DE-600)1460391-3 0014-5793 nnns volume:208 year:1986 number:2 pages:435-438 http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 208 1986 2 435-438 |
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type 1 m protein of streptococcus pyogenes - n-terminal sequence and peptic fragments |
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Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments |
| abstract |
Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. |
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Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. |
| abstract_unstemmed |
Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes. |
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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">NLEJ173303943</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705183734.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070505s1986 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ173303943</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ173303943</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">Type 1 M protein of Streptococcus pyogenes - N-terminal sequence and peptic fragments</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1986</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">Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M"r 20270 as the main product which covers the N-terminal part of the M protein. The amino acid sequence was determined of the N-terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N-terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N-terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes.</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">Moravek, L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kuhnemund, O.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Havlicek, J.V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kopecky, P.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pavlik, M.</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">208(1986), 2, Seite 435-438</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:208</subfield><subfield code="g">year:1986</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:435-438</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)81064-X</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">208</subfield><subfield code="j">1986</subfield><subfield code="e">2</subfield><subfield code="h">435-438</subfield></datafield></record></collection>
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