Details

Autor(en) / Beteiligte

• Chandra, S
• Triantaphyllopoulos, D C

Titel

Preparation of degradation products of fibrinogen free of plasmin, and their effect on thrombin activity

Ist Teil von

• Canadian journal of physiology and pharmacology, 1972-07, Vol.50 (7), p.655-661

Ort / Verlag

Canada

Erscheinungsjahr

1972

Quelle

MEDLINE

Beschreibungen/Notizen

• Sepharose 4B, a beaded agarose gel, was first activated with cyanogen bromide and then covalently coupled with pancreatic or soybean trypsin inhibitor. The degradation products of plasmin-lysed fibrinogen (DPF) were filtered through the coupled gel and the contaminating plasmin was removed by binding with the coupled inhibitor.The plasmin-free DPF thus obtained were used to study their effect on the clotting activity of thrombin. Chromatographed human thrombin was incubated in siliconized and nonsiliconized glass tubes with: (a) plasmin-free DPF, (b) albumin, (c) ceruloplasmin, and (d) saline. The activity of thrombin declined rapidly in the saline control, less so in the presence of albumin and ceruloplasmin (especially in siliconized glass tubes), and remained unchanged in the presence of DPF both in siliconized and nonsiliconized tubes. In order to study the effect of plasmin-free DPF on the inactivation of thrombin by antithrombin III, thrombin was first mixed with saline or DPF and then added to heat-defibrinated plasma (supplier of antithrombin III). The residual thrombin activity was subsequently determined at frequent intervals and was found to decline at the same rate both in the presence and in the absence of DPF. These findings demonstrate that DPF protect thrombin from spontaneous inactivation but fail to protect it against inactivation by antithrombin III.