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Biochem Biophys Res Commun. 1986 May 29;137(1):431-6.

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).

PMID:
3755044
DOI:
10.1016/0006-291x(86)91228-3
[Indexed for MEDLINE]

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