Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains.
A molecular model for the structure of human ceruloplasmin is proposed that is based on the determination of the complete amino acid sequence, studies of the products of limited proteolytic cleavage, calculations of the hydrophilic/hydrophobic character (hydropathy profile), and predictions of the l...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1984
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC391570/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6589622/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.81.15.4761 |
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