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The effect of residue 1106 on the thioester-mediated covalent binding reaction of human complement protein C4 and the monomeric rat alpha-macroglobulin alpha 1 I3

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  • X D Ren, Denmark
  • A W Dodds, Denmark
  • J J Enghild
  • C T Chu, Denmark
  • S K Law, Denmark
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
The histidine at position 1106 of the C4B isotype of human complement is involved in catalyzing the covalent binding of the thioester to glycerol and water. By replacing the histidine with other residues, it was found that tyrosine is also capable of mediating the reaction. We propose that they act as nucleophiles by first attacking the thioester, upon activation, to form acyl intermediates, which subsequently react with the hydroxyl groups of glycerol or water. The monomeric alpha-macroglobulin, alpha 1I3 of the rat, was also studied. Unlike alpha 2-macroglobulin, which is a tetramer, alpha 1I3 has binding properties similar to those of C4A.
Original languageEnglish
JournalF E B S Letters
Volume368
Issue1
Pages (from-to)87-91
Number of pages4
ISSN0014-5793
Publication statusPublished - 1995

    Research areas

  • Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Complement C4, DNA, Guinea Pigs, Histidine, Hydrogen-Ion Concentration, Protein Binding, Rats, Recombinant Proteins, Sheep, Sulfhydryl Compounds, alpha-Macroglobulins

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