Premium
Determination of the disulphide bridge arrangement of bovine histidine‐rich glycoprotein
Author(s) -
Sorensen Charlotte B.,
Krogh-Pedersen Helene,
Petersen Torben E.
Publication year - 1993
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(93)80945-q
Subject(s) - cystine , chemistry , histidine , glycoprotein , biochemistry , peptide sequence , cysteine , sequence (biology) , amino acid , enzyme , gene
Histidine‐rich glycoprotein (HRG) was purified from bovine plasma and the disulphide bridge arrangement established. Disulphide‐bridged peptides were obtained from peptic and tryptic degradation of native bovine HRG. Twelve half‐cystine residues were found in bovine HRG (compared to sixteen cysteines in human HRG), all involved in the formation of six disulphide bridges connecting Cys‐1 to Cys‐12, Cys‐2 to Cys‐3, Cys‐4 to Cys‐5, Cys‐6 to Cys‐11, Cys‐7 to Cys‐8, and Cys‐9 to Cys‐10. Additional sequence analysis of 14 C‐carboxymethylated chymotryptic and Staphylococcus aureus V8 protease generated peptides and CNBr‐fragments of bovine HRG yielded a partial amino acid sequence of bovine HRG constituting 78% of the sequence when compared to the human cDNA sequence.