Isolation and characterization of a partial cDNA clone for heparin cofactor II

Roger C. Inhorn, Douglas M. Tollefsen

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14 Scopus citations

Abstract

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).

Original languageEnglish
Pages (from-to)431-436
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume137
Issue number1
DOIs
StatePublished - May 29 1986

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