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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...

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Autores principales: Speicher, D W, Morrow, J S, Knowles, W J, Marchesi, V T
Formato: Artigo
Lenguaje:Inglês
Publicado: 1980
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC350131/
https://ncbi.nlm.nih.gov/pubmed/7003593
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