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Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components.

Publication ,  Journal Article
Sullivan, B; Bonaventura, J; Bonaventura, C; Godette, G
Published in: The Journal of biological chemistry
December 1976

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 amino acid compositions are remarkably similar to each other and to other arthropod and molluscan hemocyanins. Digestion of the native subunits of Limulus hemocyanin by formic acid or trypsin shows considerable structural diversity which is supported by cyanogen bromide cleavage patterns and by peptide mapping of the tryptic peptides prepared from denatured hemocyanin subunits. The structural differentiation of the subunits is accompanied by functional differentiation, as shown in previous investigations of their O2 and CO affinities (Sullivan, B., Bonaventura, J., and Bonaventura, C. (1974) Proc. Natl. Acad. Sci. U.S.A. 71, 2558-2562; Bonaventura, C., Bonaventura, J., Sullivan, B., and Bourne, S. (1975) Biochemistry 13, 4784-4789). The subunit diversity of Limulus hemocyanin suggests that other electrophoretically heterogeneous hemocyanins may be composed of structurally distinct subunits.

Duke Scholars

Published In

The Journal of biological chemistry

DOI

EISSN

1083-351X

ISSN

0021-9258

Publication Date

December 1976

Volume

251

Issue

23

Start / End Page

7644 / 7648

Related Subject Headings

  • Trypsin
  • Peptide Fragments
  • Molecular Weight
  • Horseshoe Crabs
  • Hemocyanins
  • Electrophoresis, Polyacrylamide Gel
  • Biochemistry & Molecular Biology
  • Arthropods
  • Animals
  • Amino Acids
 

Citation

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Sullivan, B., Bonaventura, J., Bonaventura, C., & Godette, G. (1976). Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components. The Journal of Biological Chemistry, 251(23), 7644–7648. https://doi.org/10.1016/s0021-9258(17)32900-9
Sullivan, B., J. Bonaventura, C. Bonaventura, and G. Godette. “Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components.The Journal of Biological Chemistry 251, no. 23 (December 1976): 7644–48. https://doi.org/10.1016/s0021-9258(17)32900-9.
Sullivan B, Bonaventura J, Bonaventura C, Godette G. Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components. The Journal of biological chemistry. 1976 Dec;251(23):7644–8.
Sullivan, B., et al. “Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components.The Journal of Biological Chemistry, vol. 251, no. 23, Dec. 1976, pp. 7644–48. Epmc, doi:10.1016/s0021-9258(17)32900-9.
Sullivan B, Bonaventura J, Bonaventura C, Godette G. Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components. The Journal of biological chemistry. 1976 Dec;251(23):7644–7648.

Published In

The Journal of biological chemistry

DOI

EISSN

1083-351X

ISSN

0021-9258

Publication Date

December 1976

Volume

251

Issue

23

Start / End Page

7644 / 7648

Related Subject Headings

  • Trypsin
  • Peptide Fragments
  • Molecular Weight
  • Horseshoe Crabs
  • Hemocyanins
  • Electrophoresis, Polyacrylamide Gel
  • Biochemistry & Molecular Biology
  • Arthropods
  • Animals
  • Amino Acids