[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.

Isolation of the prothrombin-converting enzyme from fibrinogenolytic enzymes of Echis carinatus venom by chromatographic and electrophoretic methods.

Chromatography of crude Echis carinatus venom revealed four enzymes with fibrinogenolytic activity and activity to chromogenic substrates, specific for proteases of the coagulation and fibrinogenolytic systems. By employing three-step chromatography on DEAE-Sephacel and Sephacryl S-200, this venom afforded the procoagulation enzyme Ecarin in good recovery (73%) and purification (53-fold). This highly purified preparation has proved to be a single-chain glycoprotein, occurring in two isomers differing in electrical charge and having a low fibrinogenolytic activity.

The chemotherapy of C3H mice bearing Gardner lymphosarcoma with bovine fibrinogen-methotrexate derivative.

Derivative of bovine fibrinogen (FBG) containing chemically bound methotrexate (MTX) has been prepared by action of ethyldimethylaminopropyl carbodiimide. The derivative retained its solubility and clotability. Intraperitoneally administered FBG-MTX derivative one day after transplantation of the ascitic Gardner lymphosarcoma prolonged distinctly the survival of C3H mice.

[Binding of butocin to serum proteins (author's transl)].

The binding of N-[-5-(6-purinylthio)-valeryl]-glycin ethylester (butocin, PVG) to serum proteins and pure human albumin was studied using the method of equilibrium dialysis. Its binding to protein in sera diluted 1:1 of 10 patients with malignant disease averaged 48.4 +/- 7.

The interaction of human hemoglobin with erythrosin. Comparison of hemoglobins with variously liganded heme groups.

The interactions of erythrosin with deoxyhemoglobin, oxyhemoglobin, carbonmonoxyhemoglobin, methemoglobin, cyanomethemoglobin and hemoglobin alpha and beta chains have been studied by using the equilibrium dialysis, the difference and circular dichroic (CD) spectra and stopped-flow method. The values of equilibrium and kinetic parameters, as well as CD characteristics, show that in addition to a number of weak binding sites hemoglobin contain four, relatively strong binding sites, one per chain. The properties of the strong binding sites depend on the ligand of the heme group and the charge of the heme group is not directly responsible for this fact.

A new simple method for determination of erythrocyte filtrability.

A new simple filtration technique designed for measuring red cell filtrability in the routine laboratory use was developed. The suspension of the whole blood in saline (1:20,000 dilution) was processed on the Sartorius filter membranes, pore size 8 micron. The percentage of passed erythrocytes indicating red cell filtrability was determined.

On the molecular conformation of human haemopexin. I. Reactivity of the tyrosine and tryptophan side chains.

The reactivity of the aromatic side chains of Tyr and Trp in human haemopexin were studied by chemical modifications and analysis of spectrophotometric titration curves. It has turned out that: 1. Under non-denaturing conditions the aromatic rings of Tyr resisted both acetylation and nitration.

[Globulinopathy and hyperuricemia].

Investigation of the locomotor system of 20 patients is reported. One patient with arthrosis of the hip joint and concomitant osteonecroses had a myeloma. In 5 RA patients the manifestations of secondary amyloidosis are described.

Dissolution of noncovalently bonded fibrin in the presence of bromide ions.

Two peaks were demonstrated after gel chromatography on Sepharose 6-B of noncovalently bonded firbrin dissolved in 1 M NaBr at pH 5.3. One was eluted at the void volume while the other one was eluted at the elution volume of fibrinogen.

The binding of chloramphenicol to serum proteins in patients with chronic renal insufficiency.

The binding (r) of chloramphenicol to serum proteins is significantly lower in patients with chronic renal failure than in normal subjects. Before hemodialysis, the mean r value in patients with chronic renal insufficiency was 0.165 mg/g (+/-0.