Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis
We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifuga...
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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, 332(1974), 2, Seite 175-191 |
| Übergeordnetes Werk: |
volume:332 ; year:1974 ; number:2 ; pages:175-191 |
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NLEJ185740057 |
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| 245 | 1 | 0 | |a Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis |
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| 520 | |a We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. | ||
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| 700 | 1 | |a Fischer, H. |4 oth | |
| 700 | 1 | |a Wallach, D.F.H. |4 oth | |
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(DE-627)NLEJ185740057 (DE-599)GBVNLZ185740057 DE-627 ger DE-627 rakwb eng Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Schmidt-Ullrich, R. oth Ferber, E. oth Knufermann, H. oth Fischer, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 332(1974), 2, Seite 175-191 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:332 year:1974 number:2 pages:175-191 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90372-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 332 1974 2 175-191 |
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(DE-627)NLEJ185740057 (DE-599)GBVNLZ185740057 DE-627 ger DE-627 rakwb eng Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Schmidt-Ullrich, R. oth Ferber, E. oth Knufermann, H. oth Fischer, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 332(1974), 2, Seite 175-191 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:332 year:1974 number:2 pages:175-191 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90372-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 332 1974 2 175-191 |
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(DE-627)NLEJ185740057 (DE-599)GBVNLZ185740057 DE-627 ger DE-627 rakwb eng Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Schmidt-Ullrich, R. oth Ferber, E. oth Knufermann, H. oth Fischer, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 332(1974), 2, Seite 175-191 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:332 year:1974 number:2 pages:175-191 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90372-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 332 1974 2 175-191 |
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(DE-627)NLEJ185740057 (DE-599)GBVNLZ185740057 DE-627 ger DE-627 rakwb eng Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Schmidt-Ullrich, R. oth Ferber, E. oth Knufermann, H. oth Fischer, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 332(1974), 2, Seite 175-191 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:332 year:1974 number:2 pages:175-191 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90372-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 332 1974 2 175-191 |
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(DE-627)NLEJ185740057 (DE-599)GBVNLZ185740057 DE-627 ger DE-627 rakwb eng Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Schmidt-Ullrich, R. oth Ferber, E. oth Knufermann, H. oth Fischer, H. oth Wallach, D.F.H. oth in Biochimica et Biophysica Acta (BBA)/Biomembranes Amsterdam : Elsevier 332(1974), 2, Seite 175-191 (DE-627)NLEJ185706983 (DE-600)2209384-9 0005-2736 nnns volume:332 year:1974 number:2 pages:175-191 http://linkinghub.elsevier.com/retrieve/pii/0005-2736(74)90372-1 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 332 1974 2 175-191 |
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analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis |
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Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis |
| abstract |
We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. |
| abstractGer |
We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. |
| abstract_unstemmed |
We have purified the plasma membranes and membranes of endoplasmic reticulum from calf and rabbit thymocytes and from calf mediastinal lymph node lymphocytes. We disrupted the cells by the ''nitrogen cavitation method'' and prepared a microsomal isolate by differential centrifugation. We fractionated this by isopycnic ultracentrifugation in dextran gradients into membrane vesicles, PM"1 and PM"2, most likely derived from plasma membrane and a fraction, ER, most likely originating from endoplasmic reticulum. More than 80% of the microsomal 5'-nucleotidase and acid p-nitrophenylphosphatase concentrates in the PM"1 and PM"2 fractions; alkaline p-nitrophenylphosphatase, another presumptive PM marker, is concentrated in the PM"1 fraction. These data are confirmed by the lacroperoxidase radioiodination of intact rabbit thymocytes followed by subcellular fractionation. The specific content of phospholipids (822 nmoles/mg protein) and cholesterol (1032 nmoles/mg protein) is highest in PM"1 and PM"2 plasma membrane fractions. NADH-oxidoreductase, our endoplasmic reticulum marker, is clearly enriched in gradient pellet.The membrane proteins were separated by electrophoretic molecular sieving in sodium dodecylsulfate-polyacrylamide gel electrophoresis, containing dithiothreitol (sodium dodecylsulfate-polyacrylamide gel electrophoresis). We numbered the 10 major protein components of the ''microsomal fraction'' (apparent molecular weights between 280000 and 15000) from 1-10 according to their decreasing molecular weights. Of these proteins, those with higher molecular weight, predominantly glycoproteins, appear in the PM"1 fraction, while the endoplasmic reticulum fraction contains mainly low molecular weight components. |
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Analysis of the proteins in thymocyte plasma membrane and smooth endoplasmic reticulum by sodium dodecylsulfate-gel electrophoresis |
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Schmidt-Ullrich, R. Ferber, E. Knufermann, H. Fischer, H. Wallach, D.F.H. |
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