Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation

Biochem J. 1988 Jul 15;253(2):615-8. doi: 10.1042/bj2530615.

Abstract

Simple rapid procedures for identification and analysis of dysfunctional C1-inhibitor proteins mutated at the reactive-centre P1 residue have been developed and used to define structurally a C1-inhibitor protein, C1-inhibitor(At), isolated from an individual with hereditary angio-oedema. The observed mutation, Arg444----His, is compatible with a single base change in the codon used for Arg444 in the native protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angioedema / blood*
  • Angioedema / genetics
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Complement C1 Inactivator Proteins*
  • Electrophoresis, Polyacrylamide Gel
  • Histidine / analysis
  • Humans
  • Molecular Sequence Data
  • Mutation

Substances

  • Complement C1 Inactivator Proteins
  • Histidine