Cobalt(II)-substituted Horseshoe Crab Hemocyanins

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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 abolishes both the reverse Bohr effect and cooperative oxygen binding. Chloride ions interact wit...

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Hemocyanin of the Horseshoe Crab, Limzdus polyphemus

The high molecular weight hemocyanin found in the hemolymph of the horseshoe crab, Limulus polyphemus, is composed of at least eight different kinds of subunits. Ion exchange chromatography at high pH in the presence of EDTA yields five major zones, hemocyanins I to V, three of which are electrophoretically heterogeneous. The subunits have similar molecular weights, 65,000 to 70,000, and their ...

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ژورنال

عنوان ژورنال: Bulletin of the Chemical Society of Japan

سال: 1982

ISSN: 0009-2673,1348-0634

DOI: 10.1246/bcsj.55.212