Anticoagulant activity of a bacterial glycopeptide.

Abstract:

:The anticoagulant properties of myxalin, a glycopeptide secreted by a Gram negative bacterium strain (Myxococcus xanthus) are studied and compared to those of heparin. This soluble material exhibits an anticoagulant activity which implies the inhibition of some serine proteases, thrombin and factor Xa. In the presence of normal and antithrombin III-depleted plasma, myxalin inhibits the amidolytic activity of thrombin on synthetic chromogenic substrate as a function of its concentration, but fails to increase thrombin inactivation significantly in the presence of purified AT III. However, crossed immunoelectrophoresis data suggests that its antithrombi effect is mainly mediated by binding to the enzyme, rather than to AT III and probably differs from the catalytic activity of heparin which requires the presence of AT III. The anticoagulant process occurs without degradation of fibrinogen and can be neutralized by protamine.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Akoum A,Josefonvicz J,Sigot M

doi

10.1016/0049-3848(90)90335-a

subject

Has Abstract

pub_date

1990-10-01 00:00:00

pages

9-18

issue

1

eissn

0049-3848

issn

1879-2472

pii

0049-3848(90)90335-A

journal_volume

60

pub_type

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