Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation.
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.
Aulak
K S
KS
MIP Unit, MRC Centre, Cambridge, U.K.
Pemberton
P A
PA
Rosen
F S
FS
Carrell
R W
RW
Lachmann
P J
PJ
Harrison
R A
RA
D000595:Amino Acid Sequence; D000799:Angioedema / Q000097:blood* / Q000235:genetics; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D003174:Complement C1 Inactivator Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006639:Histidine / Q000032:analysis; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation
D003174:Complement C1 Inactivator Proteins; D006639:Histidine