-
A new member of the plasma protease inhibitor gene family.
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.
PMID: 3003690 [PubMed - indexed for MEDLINE]
PMCID: PMC339484
-
Cited by 4 PubMed Central articles
-
ReviewGlycosaminoglycans and the regulation of blood coagulation.
Bourin MC, Lindahl U.
Biochem J. 1993 Jan 15; 289 ( Pt 2):313-30.
[Biochem J. 1993]
-
Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation.
Suzuki K, Kusumoto H, Deyashiki Y, Nishioka J, Maruyama I, Zushi M, Kawahara S, Honda G, Yamamoto S, Horiguchi S.
EMBO J. 1987 Jul; 6(7):1891-7.
[EMBO J. 1987]
-
Anti-thrombin activities of heparin. Effect of saccharide chain length on thrombin inhibition by heparin cofactor II and by antithrombin.
Bray B, Lane DA, Freyssinet JM, Pejler G, Lindahl U.
Biochem J. 1989 Aug 15; 262(1):225-32.
[Biochem J. 1989]
- » See all...