PubMed Health⌕ Search

Biomedical subjects

T Jakab

Publications and source records attributed to T Jakab.

18 recordsLinked to original sources

[The fibrin and plasma-protein content of human thrombi].

The protein composition of cell-free thrombus contained in abdominal aneurysms of the aorta was investigated using PAGE and immunoreactivity after solubilization. 1. The dry weight was 18--29%, with minor differences between various locations. 2. 35--40% of the dry weight was extractable with NaCl/citrate and was identified as albumin (80%) and IgG (15%). Trace amounts of fibrinogen immunoreactive material were present. 3. The NaCl/citrate insoluble part was 80% hydrolyzable with plasmin. The predominant fragment was D-D dimer (from cross-linked fibrin). In addition, fragments Dand E were observed. Reduction of the NaCl/citrate insoluble part with 2-mercaptoethanol resulted in almost complete solubilization. PAGE analysis demonstrated alpha-polmers, gamma-gamma dimers and little free alpha-chains, indicating almost complete cross-linking of fibrin. Thus, the major protein were cross-linked fibrin, albumin and IgG.

Aortic Aneurysm↗

Effects of amidination and chemical cross-linking on human factor VIII (antihemophilic factor).

The bifunctional reagent dimethyl suberimidate, reacting with primary amino groups of proteins, was used to cross-link highly purified human factor VIII. Reaction products were reduced with beta-mercaptoethanol or treated with Rhizopus arrhizus triglyceride lipase. The proportions of the dissociated subunits and their oligomers were calculated from the relative staining intensities of individual bands following polyacrylamide electrophoresis in the presence of sodium dodecyl sulfate. Low concentrations of dimethyl suberimidate (up to 0.5 mM) produced covalently linked dimers which retained full functional (coagulant and von Willebrand factor) activities. Treatment with increasing concentrations of dimethyl suberimidate resulted in an almost simultaneous appearance of both trimeric and tetrameric species, suggesting the existence of specific intra-dimer contacts. A parallel decrease of functional activities was observed at higher concentrations of dimethyl suberimidate. A monofunctional reagent (ethyl acetimidate), reacting similarly with primary amino groups, amidinated factor VIII at rates similar to dimethyl suberimidate. Up to 40% amidinated factor VIII retained full biological activities. We conclude that the most reactive lysine residues are not involved in the active sites responsible for either coagulant or von Willebrand activity.

Blood Coagulation↗

Variable degradation of factor VIII-related protein in lyophilised concentrates of antihaemophilic factor (AHF).

Factor VIII-related properties (coagulant = VIII : C, 'Willebrand' factor = VIII R : WF, antigen = VIII R : AG) are measured in a constant proportion in normal plasma and certain preparations of highly purified factor VIII (relative ratios: 0.5--1.5). We tested these activities in some commercial, lyophilised concentrates of factor VIII and found a variable increase of the ratio VIII R : AG/VIII R : WF. The relative increase of VIII R : AG, and/or loss of VIII R : WF, was attributed to variable degradation of factor VIII-related protein(s) which was directly visualized by electrophoresis on 2.75% polyacrylamide gels in the presence of sodium dodecyl sulphate.

Antigens↗

[Study of nasal function by the spirographic method].

The authors performed spirographic investigations of respiration through the mouth, through both nostrils and separately through the right and the left nostrie in 44 people with normal anatomy of the nose. They discuss the methods applied as well as the physiologic changes in the respiratory function of the nose. They point out the practical importance of their study.

Humans↗