Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases
We report the isolation of the human gene encoding an inhibitor of neutrophil elastase and cathepsin G. We have sequenced the gene and a cDNA clone isolated from human parotid tissue. The protein encoded by this gene appears to contain two functional domains, one having a trypsin inhibitory site and...
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Veröffentlicht in: | Nucleic acids research 1986-10, Vol.14 (20), p.7883-7896 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | We report the isolation of the human gene encoding an inhibitor of neutrophil elastase and cathepsin G. We have sequenced the gene and a cDNA clone isolated from human parotid tissue. The protein encoded by this gene appears to contain two functional domains, one having a trypsin inhibitory site and the other an elastase inhibitory site. The two-domain structure of the protein is reflected in the organization of the gene, with each domain represented by a separate exon. We have also noted that the intervening sequence separating the trypsin-inhibitor-exon and the elastase-inhibitor-exon is flanked by eleven base-pair direct repeats, suggesting that this intron may have been generated by a transposition-type event. |
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ISSN: | 0305-1048 1362-4962 |
DOI: | 10.1093/nar/14.20.7883 |