The action of pepsin on porcine immunoglobulin M and its effect on biological activity

D Beale, J K Fazakerley

Research output: Contribution to journalArticlepeer-review

Abstract

Treatment of porcine immunoglobulin M (IgM) with pepsin at pH 4.6 and 37 degrees C was found to gradually remove Fab arms and Cmicro2 domains over a period of 18h. Structural studies failed to find any other change. The main products can therefore be regarded as IgM-like molecules with limited numbers of Fab arms and Cmicro2 domains. Results indicated that this removal of Fab arms is probably a random process. As the average number of Fab arms per molecule was decreased the ability to agglutinate Salmonella oranienburg (mt-H) gradually diminished. Complement fixation by the complexes however, decreased rapidly, and became negligible when the average number of Fab arms was four. This was confirmed by using a preparation containing mainly molecules with three or four Fab arms. The overall results showed that molecules with three or four Fab arms can agglutinate Salmonella but that these complexes do not fix complement. Molecules with five arms probably behave like those with four. Complexes formed by molecules with six arms fix complement quite efficiently. Possible explanations for these results are discussed.
Original languageEnglish
Pages (from-to)183-91
Number of pages9
JournalBiochemical Journal
Volume191
Issue number1
Publication statusPublished - 1 Oct 1980

Keywords

  • Agglutination
  • Animals
  • Chemical Phenomena
  • Chemistry
  • Complement Fixation Tests
  • Electrophoresis, Polyacrylamide Gel
  • Immunoglobulin Fab Fragments
  • Immunoglobulin M
  • Molecular Weight
  • Pepsin A
  • Salmonella
  • Structure-Activity Relationship
  • Swine
  • Ultracentrifugation

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