Sulfation of tyrosine residues increases activity of the fourth component of complement.
Sulfation of tyrosine residues recently has been recognized as a biosynthetic modification of many plasma proteins and other secretory proteins. Effects of this site-specific modification on protein function are not known, but the activity of several peptides such as cholecystokinin is greatly augme...
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| Udgivet i: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
1989
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC286685/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2919182/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.4.1338 |
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