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Amino acid sequence of the N‐terminal region of human hemopexin
Author(s) -
Frantíková Věra,
Borvák Josef,
Kluh Ivan,
Morávek Ladislav
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80603-1
Subject(s) - hemopexin , terminal (telecommunication) , peptide sequence , sequence (biology) , chemistry , amino terminal , amino acid , biochemistry , stereochemistry , computational biology , biology , gene , computer science , enzyme , heme , telecommunications
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.