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Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site.
Structural studies of the human transferrin receptor have shown that the molecule is a disulfide-bonded dimer consisting of two identical subunits (Mr = 95,000) which are post-translationally modified by the addition of a fatty acyl moiety. Oligonucleotide site-directed mutagenesis has been used to...
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| Publicado no: | EMBO J |
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| Main Authors: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group
1987
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC553399/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3582362/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1987.tb04758.x |
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