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FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a <t>phosphorimager</t> (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.
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FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a <t>phosphorimager</t> (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.
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FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a <t>phosphorimager</t> (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.
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FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a <t>phosphorimager</t> (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.
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Image Search Results


FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a phosphorimager (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.

Journal: Journal of Virology

Article Title: Mapping the Golgi Targeting and Retention Signal of Bunyamwera Virus Glycoproteins

doi: 10.1128/jvi.78.19.10793-10802.2004

Figure Lengend Snippet: FIG. 4. Endo H resistance of BUN glycoproteins. Vero E6 cells were infected with vTF7-3 and subsequently transfected with the pa- rental BUN M segment cDNA (pTM-BUNM) and mutants carrying internal deletions as indicated. The cells were radiolabeled with [35S]methionine, and radiolabeled proteins were immunoprecipitated with an anti-BUN antiserum. The resulting precipitates were subjected to digestion with endo H (H) or PNGase F (F) as shown and were analyzed by SDS–10% PAGE under reducing conditions. The trun- cated Gn proteins expressed from M cDNA mutants are marked with asterisks. The gel was exposed to a phosphorimager (Molecular Im- ager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software.

Article Snippet: The gel was exposed to a phosphorimager (Molecular Imager FX; Bio-Rad Laboratories), and the relative intensities of the two forms of Gc were estimated from a computer-enlarged image by the use of Quantity One (v. 4.2.2) software. on M ay 26, 2015 by N Y U M E D IC A L C E N T E R LIB R A R Y http://jvi.asm .org/ D ow nloaded from it induces fusion between the plasma membranes of adjacent cells, leading to syncytium formation (40).

Techniques: Infection, Transfection, Immunoprecipitation, Software