Studies onthe chemical nature of lysine-binding sites and on their localization in human plasminogen.
The isolated 'kringle' structures 1 and 4 of human plasminogen lost lysine affinity upon photo-oxidation of histidine, but mostly retained it in the presence of 6-aminohexanoic acid. Lysine affinity was lost and could be partially restored after blocking of histidine with diethylpyrocarbonate and deblocking, or after esterification of COOH-groups and saponification. Only His-31 and most likely Asp-54 qualify as participants in a lysine binding site when the primary structures of the 'kringles' are considered.
D000595:Amino Acid Sequence; D001665:Binding Sites; D006639:Histidine; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008956:Models, Chemical; D008968:Molecular Conformation; D010777:Photochemistry; D010958:Plasminogen / Q000378:metabolism*
D006639:Histidine; D010958:Plasminogen; D008239:Lysine