The structure of arthropod hemocyanins.

@article{Linzen1985TheSO,
  title={The structure of arthropod hemocyanins.},
  author={Bernt Linzen and Nell M. Soeter and Austen F. Riggs and H. J. Schneider and W. Schartau and Margaret D. Moore and Eisaku Yokota and Peter Behrens and Hiroyuki Nakashima and Tetsuo Takagi},
  journal={Science},
  year={1985},
  volume={229 4713},
  pages={
          519-24
        }
}
Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely with the three domain structure established by x-ray crystallography for spiny lobster hemocyanin. The degree of identity is particularly… CONTINUE READING
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