A new member of the plasma protease inhibitor gene family
- 26 January 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 14 (2) , 1073-1088
- https://doi.org/10.1093/nar/14.2.1073
Abstract
A 2.1-kb cDNA clone representing a new member of the protease inhibitor family was isolated from a human liver cDNA library. The inhibitor, named human Leuserpin 2 (hLS2), comprises 480 amino acids and contains a leucine residue at its putative reactive center. HLS2 is about 25-28% homologous to three human members of the plasma protease inhibitor family: antithrombin III, alpha 1-antitrypsin and alpha 1-antichymotrypsin. A comparison with published partial amino acid sequences shows that hLS2 is closely related to the thrombin inhibitor heparin cofactor II.Keywords
This publication has 51 references indexed in Scilit:
- Molecular cloning of a cDNA encoding human antihaemophilic factorNature, 1984
- Primary structure of human preangiotensinogen deduced from the cloned cDNA sequenceBiochemistry, 1984
- Sequence homology between human .alpha.1-antichymotrypsin, .alpha.1-antitrypsin, and antithrombin IIIBiochemistry, 1983
- Mutation of Antitrypsin to AntithrombinNew England Journal of Medicine, 1983
- Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema.Journal of Clinical Investigation, 1981
- The ovalbumin gene family: Structure of the X gene and evolution of duplicated split genesCell, 1980
- A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha1-proteinase inhibitorBiochemical and Biophysical Research Communications, 1980
- Trans-complementable copy-number mutants of plasmid ColE1Nature, 1980
- The use of thin acrylamide gels for DNA sequencingFEBS Letters, 1978
- 3′ Non-coding region sequences in eukaryotic messenger RNANature, 1976