Studies onthe chemical nature of lysine-binding sites and on their localization in human plasminogen

Biochim Biophys Acta. 1980 Oct 21;625(2):374-8. doi: 10.1016/0005-2795(80)90302-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Histidine
  • Humans
  • Lysine / metabolism*
  • Models, Chemical
  • Molecular Conformation
  • Photochemistry
  • Plasminogen / metabolism*

Substances

  • Histidine
  • Plasminogen
  • Lysine