Literature DB >> 3488058

Isolation and analysis of a cDNA coding for human C1 inhibitor.

B G Que, P H Petra.   

Abstract

A cDNA coding for C1 inhibitor was isolated from a human liver lambda gt11 expression library and sequenced by the dideoxy method. The amino acid sequence deduced from the cDNA indicated that the insert was a partial clone coding for 310 amino acids including the reactive site present at the carboxyl end of the molecule. The reactive site corresponds to that previously reported by Salvesen et al. (J. Biol. Chem. 260, 2432, 1985). The cDNA also contained a stop codon of TGA, 264 nucleotides at the 3' noncoding region, and a polyadenylation signal sequence of AATAAA 15 nucleotides upstream from the poly(A) tail. The amino acid sequence flanking the reactive site of the inhibitor is homologous to other members of the superfamily of plasma serine protease inhibitors.

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Year:  1986        PMID: 3488058     DOI: 10.1016/0006-291x(86)91123-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

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

Authors:  K S Aulak; P A Pemberton; F S Rosen; R W Carrell; P J Lachmann; R A Harrison
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

  1 in total

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