Identification of proteolytically resistant domains of human erythrocyte spectrin.
Digestion of purified human erthrocyte spectrin with proteolytic enzymes at 0 degrees C results in the production of intermediate-size peptides that resist further cleavage at 0 degrees C. By two-dimensional peptide analysis of these intermediate peptides it has been determined that five unique pept...
Sparad:
| I publikationen: | Proc Natl Acad Sci U S A |
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| Huvudupphov: | , , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Utgiven: |
National Academy of Sciences
1980
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC350131/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7003593/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.77.10.5673 |
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