Substrate heterogeneity of component a of the human erythrocyte membrane
Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated subs...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1976 |
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| Umfang: |
1 Ill. ; 1 Tab. 6 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Supramolecular Structure - New York, N.Y. : Alan R. Liss, Inc, 4(1976) vom: Apr., Seite 481-486 |
| Übergeordnetes Werk: |
volume:4 ; year:1976 ; month:04 ; pages:481-486 ; extent:6 |
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| 520 | |a Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). | ||
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(DE-627)NLEJ159893577 DE-627 ger DE-627 rakwb eng Substrate heterogeneity of component a of the human erythrocyte membrane 1976 1 Ill. 1 Tab. 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). Wiley InterScience Backfile Collection 1832-2000 Roses, Allen D. oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 4(1976) vom: Apr., Seite 481-486 (DE-627)NLEJ159070716 0091-7419 nnns volume:4 year:1976 month:04 pages:481-486 extent:6 http://dx.doi.org/10.1002/jss.400040407 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1976 4 481-486 6 |
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(DE-627)NLEJ159893577 DE-627 ger DE-627 rakwb eng Substrate heterogeneity of component a of the human erythrocyte membrane 1976 1 Ill. 1 Tab. 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). Wiley InterScience Backfile Collection 1832-2000 Roses, Allen D. oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 4(1976) vom: Apr., Seite 481-486 (DE-627)NLEJ159070716 0091-7419 nnns volume:4 year:1976 month:04 pages:481-486 extent:6 http://dx.doi.org/10.1002/jss.400040407 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1976 4 481-486 6 |
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(DE-627)NLEJ159893577 DE-627 ger DE-627 rakwb eng Substrate heterogeneity of component a of the human erythrocyte membrane 1976 1 Ill. 1 Tab. 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). Wiley InterScience Backfile Collection 1832-2000 Roses, Allen D. oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 4(1976) vom: Apr., Seite 481-486 (DE-627)NLEJ159070716 0091-7419 nnns volume:4 year:1976 month:04 pages:481-486 extent:6 http://dx.doi.org/10.1002/jss.400040407 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1976 4 481-486 6 |
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(DE-627)NLEJ159893577 DE-627 ger DE-627 rakwb eng Substrate heterogeneity of component a of the human erythrocyte membrane 1976 1 Ill. 1 Tab. 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). Wiley InterScience Backfile Collection 1832-2000 Roses, Allen D. oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 4(1976) vom: Apr., Seite 481-486 (DE-627)NLEJ159070716 0091-7419 nnns volume:4 year:1976 month:04 pages:481-486 extent:6 http://dx.doi.org/10.1002/jss.400040407 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1976 4 481-486 6 |
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(DE-627)NLEJ159893577 DE-627 ger DE-627 rakwb eng Substrate heterogeneity of component a of the human erythrocyte membrane 1976 1 Ill. 1 Tab. 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). Wiley InterScience Backfile Collection 1832-2000 Roses, Allen D. oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 4(1976) vom: Apr., Seite 481-486 (DE-627)NLEJ159070716 0091-7419 nnns volume:4 year:1976 month:04 pages:481-486 extent:6 http://dx.doi.org/10.1002/jss.400040407 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1976 4 481-486 6 |
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Substrate heterogeneity of component a of the human erythrocyte membrane |
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Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). |
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Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). |
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Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51-58 (1975)). We have demonstrated substrate heterogeneity of two fractions of component a separated by concanavalin A (Con-A) sepharose chromatography. The fraction of component a that is retarded by Con A and eluted with α-methyl-D-glucoside does not accept the transfer of phosphate from [γ-32P] ATP as a substrate for endogenous protein kinase activity. The nonretarded fraction contains > 90% of the radioactive label. These experiments also confirm the carbohydrate heterogeneity of component a (Findley, J. B. C., J. Biol. Chem. 249:4398 (1974)). |
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