Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos
Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) prot...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1985 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Experimental Cell Research - Amsterdam : Elsevier, 156(1985), 1, Seite 7-14 |
| Übergeordnetes Werk: |
volume:156 ; year:1985 ; number:1 ; pages:7-14 |
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NLEJ184299713 |
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| 520 | |a Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. | ||
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(DE-627)NLEJ184299713 (DE-599)GBVNLZ184299713 DE-627 ger DE-627 rakwb eng Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Simone, D.W. oth SpiegeL, M. oth in Experimental Cell Research Amsterdam : Elsevier 156(1985), 1, Seite 7-14 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:156 year:1985 number:1 pages:7-14 http://dx.doi.org/10.1016/0014-4827(85)90256-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 156 1985 1 7-14 |
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(DE-627)NLEJ184299713 (DE-599)GBVNLZ184299713 DE-627 ger DE-627 rakwb eng Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Simone, D.W. oth SpiegeL, M. oth in Experimental Cell Research Amsterdam : Elsevier 156(1985), 1, Seite 7-14 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:156 year:1985 number:1 pages:7-14 http://dx.doi.org/10.1016/0014-4827(85)90256-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 156 1985 1 7-14 |
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(DE-627)NLEJ184299713 (DE-599)GBVNLZ184299713 DE-627 ger DE-627 rakwb eng Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Simone, D.W. oth SpiegeL, M. oth in Experimental Cell Research Amsterdam : Elsevier 156(1985), 1, Seite 7-14 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:156 year:1985 number:1 pages:7-14 http://dx.doi.org/10.1016/0014-4827(85)90256-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 156 1985 1 7-14 |
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(DE-627)NLEJ184299713 (DE-599)GBVNLZ184299713 DE-627 ger DE-627 rakwb eng Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Simone, D.W. oth SpiegeL, M. oth in Experimental Cell Research Amsterdam : Elsevier 156(1985), 1, Seite 7-14 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:156 year:1985 number:1 pages:7-14 http://dx.doi.org/10.1016/0014-4827(85)90256-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 156 1985 1 7-14 |
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(DE-627)NLEJ184299713 (DE-599)GBVNLZ184299713 DE-627 ger DE-627 rakwb eng Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Simone, D.W. oth SpiegeL, M. oth in Experimental Cell Research Amsterdam : Elsevier 156(1985), 1, Seite 7-14 (DE-627)NLEJ177031808 (DE-600)1466780-0 0014-4827 nnns volume:156 year:1985 number:1 pages:7-14 http://dx.doi.org/10.1016/0014-4827(85)90256-3 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 156 1985 1 7-14 |
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micromere-specific cell surface proteins of 16-cell stage sea urchin embryos |
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Micromere-specific cell surface proteins of 16-cell stage sea urchin embryos |
| abstract |
Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. |
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Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. |
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Evidence is presented of cell-type specificity of surface proteins from the 16-cell stage sea urchin embryo. The protein composition of the micromere cell surface has been examined by ^1^2^5I labelling of intact cells followed by SDS-PAGE. In Arbacia punctulata, four high molecular weight (HMW) proteins are detected on the surface of isolated micromeres-but not on mesomere-macromere fractions. In Strongylocentrotus droebachiensis, a micromere-specific protein of 133 K molecular weight (MW) was identified. This 133 K protein binds to wheat germ agglutinin (WGA) but not to concanavalin A (conA). Lectin binding was studied using a new technique. The procedure involves the separation, by SDS-PAGE, of iodinated cell-surface proteins followed by their electrophoretic transfer to lectin-coated nitrocellulose membranes. Using this procedure, celltype-specific surface proteins which are also lectin-binding-specific, were detected. |
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