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Differential reduction of interchain disulphide bonds of mouse immunoglobulin G
The relative lability of the interchain disulphide bonds of mouse G(2a)-myeloma protein 5563 was studied as a function of 2-mercaptoethanol concentration. Analysis of partial-reduction mixtures by polyacrylamide-gel electrophoresis and microdensitometry showed that the disulphide bonds between light...
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| Hauptverfasser: | , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
1968
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1198754/ https://ncbi.nlm.nih.gov/pubmed/16742608 |
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