The presence of a Ca2+ bridge within the gamma chain of human fibrinogen.
The presence of Ca2+ increased the mobility of fragment D, and the gamma chain from fibrinogen on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate, suggesting that a Ca2+ was associated with these fibrinogen derivatives. The mobilities of the constituent chains from fragment D produced under various conditions, indicate that Ca2+ bound to fibrinogen form an intrachain bridge towards the C-terminus of each gamma chain.
D001665:Binding Sites; D001952:Bridged-Ring Compounds; D002118:Calcium / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen; D006801:Humans; D008970:Molecular Weight; D010446:Peptide Fragments
D001952:Bridged-Ring Compounds; D010446:Peptide Fragments; D005340:Fibrinogen; D004492:Edetic Acid; D002118:Calcium