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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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| Autors principals: | , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
1987
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC553399/ https://ncbi.nlm.nih.gov/pubmed/3582362 |
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