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Interaction between the labile binding site of human C4 and methylamine

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Author

Summary, in English

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.

Publishing year

1981

Language

English

Pages

199-203

Publication/Series

Scandinavian Journal of Immunology

Volume

13

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • 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

Status

Published

ISBN/ISSN/Other

  • ISSN: 0300-9475