English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

To study molecular-mass dependence of dextran sulfate (DS) for interactions with several plasma proteins, a commercial preparation of the sulfated polysaccharide was fractionated by gel filtration chromatography into six subfractions with relatively different molecular masses. Simple two-component systems were available to measure the interactions of the proteins with the subfractions of DS. These were done to determine the rates of time-dependent changes in intrinsic fluorescence of thrombin and fibrinogen, and the enzyme inactivation in the presence of DS. Their interactions were also confirmed in three-component systems, in which the interactions of DS with thrombin and fibrinogen were measured by the displaced binding by FTC-heparin, and DS-enhanced proteolysis by chymotrypsin, respectively. Moreover, the neutralization of factor Xa by antithrombin III (AT III) depended on the molecular mass of DS. All the results obtained indicate that most of the general interactions of thrombin, fibrinogen, and probably AT III increased with increasing molecular mass of DS.

biological chemistry hoppe-seyler

The Molecular-Mass Dependence of Dextran Sulfate Enhancement of Inactivation of Thrombin and Fibrinogen and on Factor Xa Neutralization by Antithrombin III