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Human surfactant polypeptide SP-B. Disulfide bridges, C-terminal end, and peptide analysis of the airway form.

Human hydrophobic surfactant polypeptide, SP-B, purified from lung tissue by exclusion chromatography in organic solvents, has been characterized. The polypeptide is 79 residues long, has a C-terminal methionine, and contains seven Cys residues. Native human SP-B lacks free thiol groups. Three intrachain disulfide bridges were defined, linking Cys8 to Cys77, Cys11 to Cys71 and Cys35 to Cys46. The remaining Cys48 is concluded to link the protein chains into homodimers via an interchain disulfide to its counterpart in a second SP-B polypeptide. These SS bridges are identical to those in the porcine form and confirm a consestant and unique disulfide pattern for SP-B polypeptides in general.[1]

References

  1. Human surfactant polypeptide SP-B. Disulfide bridges, C-terminal end, and peptide analysis of the airway form. Johansson, J., Jörnvall, H., Curstedt, T. FEBS Lett. (1992) [Pubmed]
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