Interchain disulfide bonds in procollagen are located in a large nontriple-helical COOH-terminal domain.
Tadpole collagenase (EC 3.4.24.3) cleaved chick cranial bone procollagen into two triple-stranded fragments, PCA and PCB. Only PCB, with an estimated molecular weight of about 60,000 for each component chain after reduction, was found to contain interchain disulfide bonds. The analogous cleavage of...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
|---|---|
| Päätekijät: | , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
1975
|
| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC432908/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/171650/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.72.8.3009 |
| Tagit: |
Ei tageja, Lisää ensimmäinen tagi!
|