TY - JOUR
T1 - Isolation and characterization of a partial cDNA clone for heparin cofactor II
AU - Inhorn, Roger C.
AU - Tollefsen, Douglas M.
PY - 1986/5/29
Y1 - 1986/5/29
N2 - A human fetal liver cDNA library constructed in λgt11 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 exlanation 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).
AB - A human fetal liver cDNA library constructed in λgt11 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 exlanation 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).
UR - http://www.scopus.com/inward/record.url?scp=0022494210&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(86)91228-3
DO - 10.1016/0006-291X(86)91228-3
M3 - Article
C2 - 3755044
AN - SCOPUS:0022494210
SN - 0006-291X
VL - 137
SP - 431
EP - 436
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -