Interaction between the labile binding site of human C4 and methylamine

Research output: Contribution to journalArticle

Abstract

Human complement component C4 was irreversibly inactivated by low concentrations of methylamine at slightly alkaline pH. The inactivated C4 molecules lost the ability to bind to EAC1 cells but retained th capacity to participate in the formation of classical pathway C3 convertase in the fluid phase. 14C-methylamine was incorporated into the alpha-chain at a ratio of 1 mol methylamine per mol C4.

Details

Authors
External organisations
  • Uppsala University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Medicinal Chemistry

Keywords

  • Humans, Polyacrylamide Gel, Electrophoresis, Complement C4/*antagonists & inhibitors, Complement Inactivator Proteins/pharmacology, Hydrogen-Ion Concentration, Methylamines/*pharmacology, Receptors, Complement/*drug effects, Research Support, Non-U.S. Gov't
Original languageEnglish
Pages (from-to)199-203
JournalScandinavian Journal of Immunology
Volume13
Issue number2
Publication statusPublished - 1981
Publication categoryResearch
Peer-reviewedYes
Externally publishedYes

Bibliographic note

2