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Purification of the horseshoe crab hemocyanin

External protocol Created on 03 May 2014

Authors

Naxin Jiang, Nguan Soon Tan, Bow Ho, and Jeak Ling Ding

Summary

This protocol describes the isolation and purification of hemocyanin from the horseshoe crab. In the open-circulating system of the horseshoe crab, hemocyanin is the most abundant extracellular protein, constituting >90% of the total proteins. Since hemocyanin exists as a 48-mer holo-protein (MW= 3,500 kDa)1, its sheer size makes it readily separated by gel-filtration chromatography from other major plasma proteins, such as the C-reactive protein which exists as a pentamer of 150 kDa, or α-2-macroglobulin which exists as a monomer of 180 kDa2,3.

Further details

The protocol was published on Protocol Exchange in 2007. To see the entire protocol, click on the source link.

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