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Identification of a new P1 residue mutation (444Arg→Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma
Author(s) -
Aulak K.S.,
Cicardi M.,
Harrison R.A.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81494-9
Subject(s) - hereditary angioedema , c1 inhibitor , point mutation , mutant , residue (chemistry) , cysteine , histidine , chemistry , mutation , mutant protein , dysfunctional family , microbiology and biotechnology , angioedema , biochemistry , genetics , biology , medicine , gene , amino acid , enzyme , immunology , clinical psychology
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.