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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Pubblicato in:	Proc Natl Acad Sci U S A
Autori principali:	Speicher, D W, Morrow, J S, Knowles, W J, Marchesi, V T
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	National Academy of Sciences 1980
Soggetti:	Research Article
Accesso online:	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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