[The molecular structure of serum hemopexin and its role in the metabolism of hemoglobins].

Human serum haemopexine together with albumin participates in the removal of haemoglobin released into the circulation during intravascular haemolysis by a haeme bond and in its transport into parenchymal liver cells.

The use of antibody immobilized on supports coated with polyglycidyl methacrylate in saturation analysis.

A new procedure for separation of free and bound ligand in saturation analysis (e.g., radioimmunoassay, competitive protein binding analysis) is presented.

The effect of fibrinogen-methotrexate derivatives on HeLa cell growth.

Proteolytic cleavage of bovine fibrinogen with covalently bound methotrexate (MTX) was studied using four different proteolytic enzymes--trypsin, chymotrypsin, pepsin, and cathepsin D and the interaction of the modified fibrinogen (or fibrin) with HeLa cells was investigated. The presence of fibrin-MTX derivative did not induce any significant morphological alternations of cells. The fibrin-MTX derivative in the gel form was solubilized easily by the action of all proteinases investigated, hydrolysis of highly crosslinked denatured fibrin-MTX in suspension proceeded slower.

Chemical binding of folic acid and methotrexate to bovine fibrinogen.

The binding of folic acid as a model compound and methotrexate as a representative of antifolates to bovine fibrinogen with the aid of 1-ethyl-3-(3-dimethylamino-propyl)-carbodiimide was investigated in order to study the possibility of using fibrinogen as a drug carrier. Soluble modified fibrinogen derivatives containing 0.03-0.