Amino acid sequence of the N‐terminal region of human hemopexin

FEBS Letters

Morávek, Ladislav¹  Frantíková, Věra¹  Borvák, Josef¹  Kluh, Ivan¹ 

[1] Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6, Czechoslovakia

关键词: Hemopexin;    Amino acid sequence;    Heme transport;   

DOI  :  10.1016/0014-5793(84)80603-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cyanogen bromide digestion of hemopexin at its 6 methionine residues results in 7 fragments (CB1–CB7) partially connected by disulfide bridges. By sequence studies of fragments CB1-CB4 and peptides prepared by their enzyme cleavage, a continuous amino acid sequence of the N-terminal region of human hemopexin, comprising 220 amino acid residues, was determined. The presence of intramolecular disulfide bonds, connecting half-cystine residues and , was proved in fragments CB2 and CB3. Fragments CB1–CB4 include 5 sites, where hexosamine oligosaccharides are attached (positions 1,41,164, 217 and probably 223). In the sequenced region two sites sensitive to acid hydrolysis - bonds ⋯ Asp-Pro ⋯ in positions and were found. In spite of the fact that pooled material of many donors was studied, no sequence heterogeneity was discovered.

【 授权许可】

Unknown