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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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Main Authors: Sullivan, Bolling, Bonaventura, Joseph, Bonaventura, Celia
格式: Artigo
語言:Inglês
出版: 1974
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC388499/
https://ncbi.nlm.nih.gov/pubmed/4210212
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