title: Isolation and characterization of a partial cDNA clone for heparin cofactor II1.
abstract: A human fetal liver cDNA library constructed in lambda gt11 was screened with affinity-purified rabbit antibodies raised against heparin cofactor II. One positive clone was plaque purified and the cDNA insert was completely sequenced. The clone encodes the C-terminal 167 amino acid residues of heparin cofactor II as well as the entire 3'-untranslated region of the message. Proline and leucine were identified in the P2 and P1 positions of the protease cleavage site, providing a possible explanation for the ability of heparin cofactor II to inhibit both thrombin and chymotrypsin-like proteases. The coding sequence is identical to that of the recently published human leuserpin 2 (Ragg (1986) Nucl. Acids Res. 14, 1073).
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D006023:Glycoproteins / Q000235:genetics*; D015844:Heparin Cofactor II; D006801:Humans; D008099:Liver; D011480:Protease Inhibitors / Q000235:genetics; D011506:Proteins / Q000235:genetics*
chemical_list: D006023:Glycoproteins; D011480:Protease Inhibitors; D011506:Proteins; C047932:SERPIND1 protein, human; D015844:Heparin Cofactor II; D004247:DNA