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F Madaras

Publications and source records attributed to F Madaras.

8 recordsLinked to original sources
PubMed1981

Purification and characterization of the sand crab (Ovalipes bipustulatus) coagulogen (fibrinogen).

From the coagulocytes (amoebocytes) coagulogen (fibrinogen) was isolated, and purified on Sephacryl S-200. The cell homogenate contained one major protein species with a minimum molecular weight of 70,000. This protein clotted in the presence of human thrombin, human factor XIII and Ca++. The coagulogen contained no free thiol groups, however these were detectable in the reduced protein. Using the cyanoethylation procedure, it was estimated that one coagulogen molecule contained two lysine residues which participated in the cross-linking reaction. The total amino acid composition of the crab coagulogen and coagulin (fibrin) was estimated and compared with the amino acid composition of the Limulus polyphemus, lobster, (Panulirus interruptus) and porcine fibrinogen.

Amino Acids↗
PubMed1981

Automated estimation of factor Xa using the chromogenic substrate S-2222.

A rapid automated method for the estimation of factor Xa was developed using the "Centrifichem' rotary fast analyser and the substrate S-2222. The problem of interference from fibrin was overcome by performing the activation of factor X during centrifugation, so that defibrination and activation were achieved in a single step. A range of factor Xa concentrations was determined on 50 normal plasmas. This assay was correlated with a clotting assay of factor Xa using serial dilutions of normal plasma and plasma from 30 patients receiving warfarin therapy.

Adolescent↗
PubMed1979

Coagulation in the sand crab (Ovalipes bipustulatus).

The coagulation mechanism of the sand crab (O. bipustulatus) has been investigated. From the coagulocytes (amoebocytes) present in the crab haemolymph (blood), fibrinogen (coagulogen) was isolated. It was shown to be homogeneous by electrophoresis on S.D.S. polyacrylamide gel and had a molecular weight similar to the A alpha-chain of human fibrinogen. Unlike human fibrinogen. Unlike human fibrinogen it cannot be dissociated by reduction. In fibrin polymerization, a crosslinking process takes place and this process was inhibited by glycine ethyl ester. A fibrin stabilizing factor is present in the crab haemolymph and this protein was able to cross-link human fibrin in the same manner as human factor XIII.

Animals↗
PubMed1978

Isolation and insolubilisation of human F VIII by affinity chromatography.

A simple procedure has been developed for the isolation of coagulation factor VIII (F VIII) from plasma in a form which induces a monospecific antibody in rabbits. Amino acid precipitation from plasma was followed by gel filtration on Sepharose 4B and further purification was achieved by affinity chromatography on heparin-Sepharose. The material so isolated was identified by immunoelectrophoresis and lacked coagulant activity. The antiserum produced in rabbits inhibited F VIII coagulant activity and von Willebrand factor activity as measured by ristocetin platelet agglutination. The isolated IgG fraction insolubilised with CNBr-Sepharose 4B retained the ability to complex with F VIII. This complex possessed F VIII coagulant activity which could be removed in 0.6 M NaCl and dissociated in 8 M urea.

Amino Acids↗
PubMed1976

Studies on an acquired inhibition of factor VIII induced by penicillin allergy.

An inhibitor of antihaemophilic globulin has been found in association with penicillin allergy. Inhibitor activity was detected after a severe reaction of penicillin. Neutralization studies showed the activity resided in an IgG globulin with kappa light chains. Experiments with insolubilized gammaglobulin demonstrated that the activity of the inhibitor was found in a specific penicillin antibody.

Antibodies↗