Functional Differences in the Multiple Hemocyanins of the Horseshoe Crab, Limulus polyphemus L
Hemocyanin in the hemolymph of the horseshoe crab, Limulus polyphemus L., is a high-molecular-weight copper protein which binds oxygen cooperatively and shows a higher oxygen affinity at pH 7 than at pH 9. Treatment with EDTA (ethylenediaminetetra-acetate) disaggregates the hemocyanin molecules and...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1974
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC388499/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4210212/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.71.6.2558 |
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