Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes
(1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacryl...
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Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1974 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Biomembranes - Amsterdam : Elsevier, 373(1974), 2, Seite 295-307 |
| Übergeordnetes Werk: |
volume:373 ; year:1974 ; number:2 ; pages:295-307 |
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| 245 | 1 | 0 | |a Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes |
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| 520 | |a (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 | ||
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(DE-627)NLEJ185716679 (DE-599)GBVNLZ185716679 DE-627 ger DE-627 rakwb eng Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Fischer, H. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 373(1974), 2, Seite 295-307 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:373 year:1974 number:2 pages:295-307 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90153-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 373 1974 2 295-307 |
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(DE-627)NLEJ185716679 (DE-599)GBVNLZ185716679 DE-627 ger DE-627 rakwb eng Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Fischer, H. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 373(1974), 2, Seite 295-307 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:373 year:1974 number:2 pages:295-307 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90153-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 373 1974 2 295-307 |
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(DE-627)NLEJ185716679 (DE-599)GBVNLZ185716679 DE-627 ger DE-627 rakwb eng Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Fischer, H. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 373(1974), 2, Seite 295-307 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:373 year:1974 number:2 pages:295-307 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90153-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 373 1974 2 295-307 |
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(DE-627)NLEJ185716679 (DE-599)GBVNLZ185716679 DE-627 ger DE-627 rakwb eng Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Fischer, H. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 373(1974), 2, Seite 295-307 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:373 year:1974 number:2 pages:295-307 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90153-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 373 1974 2 295-307 |
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(DE-627)NLEJ185716679 (DE-599)GBVNLZ185716679 DE-627 ger DE-627 rakwb eng Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier (1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Bhakdi, S. oth Knufermann, H. oth Fischer, H. oth Hoelzl Wallach, D.F. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 373(1974), 2, Seite 295-307 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:373 year:1974 number:2 pages:295-307 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90153-9 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 373 1974 2 295-307 |
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interaction between erythrocyte membrane proteins and complement components. ii. the identification and peptide composition of complement components c3 and c4 desorbed from erythrocyte membranes |
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Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes |
| abstract |
(1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 |
| abstractGer |
(1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 |
| abstract_unstemmed |
(1) Following lysis of sheep erythrocytes with antibody plus human complement, several serum proteins can be desorbed from washed membranes by incubating these in isotonic buffer at 37 ^oC. We have analyzed these desorbed proteins by isoelectric focusing combined with sodium dodecylsulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis.(2) Crossed immunoelectrophoresis using antisera to human serum yields complex patterns of precipitation arcs, but the use of monospecific anti-C3 and anti-C4 allows us to identify these components.(3) Isoelectric focusing in polyacrylamide followed by sodium dodecylsulfatepolyacrylamide gel electrophoresis at right angels resolves the desorbed serum proteins into three major components with characteristic isoelectric points and electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gel electrophoresis. One component is serum albumin, non-specifically absorbed. Preparative isoelectric focusing followed by crossed immunoelectrophoresis shows that the other two components comprise desorbed C3 and C4 components of complement. Their isoelectric points are 5.1 and 5.7-6.2 respectively. The desorbed C3 components comprise two entities with apparent molecular weights of 160-180 000. Disulfide cleavage with dithiothreitol splits these into two major components of apparent molecular weight 80 000 and 45 000 and one minor component of 30 000. Desorbed C4 also resolves into two closely associated bands of apparent molecular weight 160 000-170 000 in sodium dodecylsulfate gel electrophoresis. Dithiothreitol treatment reduces these to subunits of apparent molecular weight 80 000, 32 000 and 30 000. Moreover, the appearance of one protein with decreased relative mobility is obserbed.(4) These data are discussed in the light of recent findings based on two-dimensional separations of membrane proteins following complement-mediated lysis. They lead us to conclude that after solubilisation of complement-treated membranes in sodium dodecylsulfate, molecular complexes consisting of membrane-bound C3 and membrane proteins persist in solution. These complexes are stabilized by the intramolecular disulfide bonds of C3 |
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Interaction between erythrocyte membrane proteins and complement components. II. The Identification and peptide composition of complement components C3 and C4 desorbed from erythrocyte membranes |
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Bhakdi, S. Knufermann, H. Fischer, H. Hoelzl Wallach, D.F. |
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