Isolation and characterization of a protein from hagfish serum that is homologous to the third component of the mammalian complement system.

The 192-kDa protein HX, a major component of serum that specifically binds to zymosan particles, was prepared from the plasma of the hagfish (Eptatretus burgeri) by ion-exchange chromatography and gel filtration. HX, present at a concentration of 0.8 mg/ml in the original plasma, was composed of two distinct subunits of 115 kDa and 77 kDa, respectively, which were linked by disulfide bonds. The protein had the same electrophoretic mobility as beta-globulin. Digestion by trypsin resulted in a specific cleavage of the 115-kDa subunit and a change in its immunoelectrophoretic mobility in the anodal direction, leaving the 77-kDa subunit intact. Treatment with SDS and urea resulted in the splitting of the 115-kDa subunits into 68-kDa and 45-kDa components, but this splitting was inhibited by pretreatment with methylamine, suggesting the presence of a thiol ester bond in the 115-kDa subunit. The amino acid composition of HX revealed a striking resemblance to that of human C3. We conclude, therefore, that the 192-kDa protein isolated in this study is analogous to C3, which plays a key role in the mammalian C system.

• Publication year

  1992

• Venue

  Journal of Immunology

• Publication date

  1992-01-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.4049/jimmunol.148.1.117PMID 1727859
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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