A new factor Xa inhibitor (lefaxin) from the Haementeria depressa leech.

Abstract:

:The salivary complex of the leech Haementeria depressa produces potent anticoagulant components. Among them, a protein named lefaxin inhibits factor Xa (FXa). Lefaxin was purified to homogeneity from dissected salivary complexes by gel filtration in Sephadex G-150 followed by two ion exchange chromatography steps in Mono-Q. Inhibition of FXa by lefaxin was demonstrated by the inhibition of its amidolytic activity, measured with chromogenic substrate S-2765 (apparent K(I) of 4 nM), and of its ability to inhibit thrombin generation in the prothrombinase complex (EC50 of 40 nM). Lefaxin has a molecular weight of 30 kDa and an isoelectric point of 5.7. It is made of a polypeptide chain whose N-terminal sequence shows no similarity with that of other FXa inhibitors (antistasin and ghilianten) isolated from leech saliva. On the other hand, the N-terminal sequence of lefaxin presents significant sequence similarity with nitric oxide carrier proteins myohemerythrin from the annelid Nereis diversicolor and prolixin S from the triatoma Rhodnius prolixus. Interestingly, prolixin S also proved to be an anticoagulant protein acting on FXa.

journal_name

Thromb Haemost

authors

Faria F,Kelen EM,Sampaio CA,Bon C,Duval N,Chudzinski-Tavassi AM

keywords:

subject

Has Abstract

pub_date

1999-11-01 00:00:00

pages

1469-73

issue

5

eissn

0340-6245

issn

2567-689X

pii

99111469

journal_volume

82

pub_type

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