RESUMEN
A new plasminogen activator has been isolated from the saliva of Rhapactor biparticeps. This product is 5% of salivary proteins and acts at an optimal pH of 7.8.P.D.F which results from its action on human fibrinogen are similar to those which are obtained with streptokinase. The modalities of action of this plasminogen activator on the fibrinogen are discussed
Asunto(s)
Activadores Plasminogénicos , SalivaRESUMEN
The study of digestive and salivary proteases of Rhapactor biparticeps, has shown hat the salivary glands of this insect are rich in proteolytic enzymes. however, the gut has none The characterisation of these enzymes on different substrates showed that they are only active on fibrinogen and pIasmatic proteins which are involved in the coagulation system. Among these fibrinolytic enzymes that has been identified and characterized, are the plasminogen activators. Their unexpected presence in he entomophagic insect is discussed
Asunto(s)
Péptido Hidrolasas , Activadores Plasminogénicos , SalivaRESUMEN
The parasitic incidence of Opius concolor [Hymenoptera, Braconidae] on a replacement host, Ceratitis capitata [Diptera,Trypetidae] was studied using polyacrylamid gel electrophoresis and immunoelectrophoresis methods. A noticeable modification of C. capitata proteins was observed when parasited by 0. concolor. But the most important phenomenon is the finding of common antigens obetween the host and the parasite. These results are discussed with regard to trophic and parasitic behaviour of the parasite
Asunto(s)
Himenópteros/parasitología , Dípteros/parasitologíaRESUMEN
Plasminogen activators are identified in the saliva of Rhapactor biparticeps using a particular technique which includes human fibrin in polyacrylamid gel.This technique is described and results are discussed according to classical methods used for fibrinolysis studies
Asunto(s)
Saliva , Activadores Plasminogénicos , GelesRESUMEN
A new fibrinolytic enzyme, isolated from the haemolymph of Rhodnius prolixus Stal [Heteroptera, Reduviidae] has been disocovered. This enzyme does not act by activating plasminogen to plasmin. However the split products obtained with this new enzyme inhibit fibrin formation in normal plasma. This enzyme seems to act specifically on the proteins involved in blood coagulation. Its origin has induced us to name it prolixase