Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma.
A new reactive-centre P1 residue mutation (444Arg----Ser), has been identified in a dysfunctional C1 inhibitor protein, C1 inhibitor(Ba), contained in a type II hereditary angioedema plasma. This substitution is compatible with a point mutation of the 444Arg codon (CGC----AGC), and represents the first non-histidine, non-cysteine P1 residue mutant described for C1 inhibitor.
Aulak
K S
KS
MRC Molecular Immunopathology Unit, MRC Centre, Cambridge, UK.
Cicardi
M
M
Harrison
R A
RA
D000595:Amino Acid Sequence; D000799:Angioedema / Q000235:genetics*; D001483:Base Sequence; D003174:Complement C1 Inactivator Proteins / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D003174:Complement C1 Inactivator Proteins; D010446:Peptide Fragments; D014357:Trypsin