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

FEBS Letters

Curstedt, Tore¹  Johansson, Jan²  Jörnvall, Hans² 

[1] Department of Clinical Chemistry, Karolinska Institutet at Danderyd Hospital, S-182 88 Danderyd, Sweden;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Surfactant polypeptide;    SP-B;    Disulfide bridge;    Structural property;   

DOI  :  10.1016/0014-5793(92)81239-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Cys^K 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 consistant and unique disulfide pattern for SP-B polypeptides in general.

【 授权许可】

Unknown