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Biomedical subjects

R Gollwitzer

Publications and source records attributed to R Gollwitzer.

At least 19 recordsLinked to original sources
PubMed1988

Limited fibrinogenolysis in stored whole blood and in fresh frozen plasma.

Measurement of the F-CB3 related antigen of the fibrinogen alpha-chain shows a time dependent increase of fibrino(geno)lysis in whole blood during storage from 70.7 +/- 16.4 pmol/ml (day 2) to 356.3 +/- 110 pmol/ml (day 39). Simultaneously PMN-elastase increases from 95 +/- 44 micrograms/l (day 2) to 3492 +/- 954 micrograms/l (day 39). The significant correlation between PMN-elastase and F-CB3 values (n = 180, r = 0.73, p less than 0.001) may reflect a relationship between the liberation of granulocyte enzymes and the extent of fibrino(geno)lysis. The isolation and separation of fibrinogen material on SDS-PAGE indicates a limited degradation of the parent fibrinogen molecule (340 kD). During storage the fraction of slightly degraded fibrinogen (300 kD) and pre-X fragment (280 kD) increases. The separation of the reduced fibrinogen material demonstrates that the limited fibrinogenolysis mainly took place in the A alpha-chain. Additional studies on fresh frozen plasma show that PMN-elastase values (98.6 +/- 41.8 micrograms/l), F-CB3 values (84.8 +/- 31.2 pmol/ml) and the SDS-PAGE pattern of the fibrinogen material are similar to the results in whole blood stored for two days.

Blood Preservation↗
PubMed1988

The role of coagulation, fibrinogenolysis and fibrinolysis in the development of fluid and clotted cadaver plasma.

Parameters for coagulation, fibrinogenolysis and fibrinolysis were measured in order to understand the formation of fluid or clotted cadaver plasma. All values found were distinctly elevated without significant differences between fluid and clotted material. The electrophoretic banding pattern of the fibrinogen and fibrin material also proved extensive coagulation and fibrinolysis in all cases. In vitro experiments in which similar electrophoretic banding patterns were obtained suggested that the development of fluid cadaver plasma depends on the activation of fibrinolysis prior to complete coagulation, and is enhanced by persistence of circulation as well as a physiological pH (7.4). In correspondence to post mortal time only an increase in elastase values was found.

Blood Coagulation↗
PubMed1988

Proteolytic cleavage of human fibrinogen by cathepsin B.

Human fibrinogen was cleaved by human liver cathepsin B in vitro. The time course of the degradation was followed by SDS-PAGE. Using activated cathepsin B in a weight ratio of enzyme to fibrinogen of 1:100 a pH optimum of 6.0 was found at 37 degrees C. For the separation of the fibrinogen degradation products a reversed phase HPLC system was used. Fibrinogen was cleaved by cathepsin B at the C-terminal side of the A alpha-chain, partially also on its N-terminal side and at the N-terminal end of the B beta-chain.

Antibodies, Monoclonal↗
PubMed1986

X-ray crystallographic and biochemical characterization of single crystals formed by proteolytically modified human fibrinogen.

Large single crystals (0.7 mm X 0.4 mm X 0.3 mm) of human fibrinogen, modified with a crude exoprotease from Pseudomonas aeruginosa, have been obtained. The crystals are orthorhombic, space group P212121, with a = 9.5 +/- 0.1 nm, b = 11.1 +/- 0.1 nm, c = 44.0 +/- 0.4 nm. Their X-ray diffraction patterns extend to beyond 1.0 nm resolution. The asymmetric unit contains one fragment of 245 kDa molecular mass made up of an intact gamma chain, a slightly shortened beta chain and an N-terminal part (about one-third) of the alpha chain. In electron micrographs of rotary-shadowed samples the crystallized particles are very similar in size and shape to the well-known trinodular form of native fibrinogen. From the unit-cell dimensions and the intensity pattern a model is proposed in which the molecules consist of two halves related by a local twofold rotation axis, and are aligned with a displacement of multiples of 1/4 of their length giving a pseudohexagonal packing scheme.

Chromatography, High Pressure Liquid↗
PubMed1984

Crosslinked fibrin derivatives and fibronectin in ascitic fluid from patients with ovarian cancer compared to ascitic fluid in liver cirrhosis.

Ascitic fluid from patients with ovarian cancer and from patients with alcohol induced liver cirrhosis were compared in respect to hematological and related parameters (content of fibrinogen and fibrin (ogen) degradation products, fibrinopeptide A, F-CB3 related antigen, ratio of crosslinked fibrin to non crosslinked fibrin (ogen), fibronectin and total protein). In tumor ascites all parameters except FPA were significantly elevated compared with cirrhosis ascites. Tumor ascites contains a six-fold higher level of fibrin (ogen) degradation products. A considerable portion of it constitute crosslinked (factor XIII induced) high molecular weight fibrin derivatives. Their content is approx. 10 times higher in tumor ascites than in cirrhosis ascites. Characterization of the crosslinked fibrin derivatives revealed the presence of fragments DD, DY, and some other fragments compatible with XY, DXD, DXY, YXY and DXX. The fibronectin content is also significantly higher in tumor ascites compared with cirrhosis ascites. The value ranges showed no overlap. The findings suggest a turnover of fibrinogen in both ascitic fluids via coagulation and fibrinolysis. In tumor ascites however, fibrinogen seems to be catabolized to a higher degree via the degradation of crosslinked fibrin.

Ascitic Fluid↗
PubMed1983

[Markerfunction of crosslinked fibrin derivatives in ascitic fluid from patients with ovarian cancer: a comparison with ascitic fluid in liver cirrhosis].

Ascitic fluid from patients with ovarian cancer contains high levels of fibrin(ogen) degradation products (FDP). Crosslinked fibrin derivatives were isolated by precipitation and separated by PAA-gel-electrophoresis. In order to evaluate the submolecular structure the total precipitate and single derivatives were investigated after cleavage of the disulfide bonds. The findings are related to the radioimmunological measurements of certain fibrinopeptides. Tumor ascites contains approximately ten times higher levels of crosslinked fibrin derivatives than cirrhosis ascites. The fibrinopeptide A content is similar, whereas the levels of plasmin-induced alpha-chain fragment are significantly higher in tumor ascites. The findings suggest a catabolism of fibrinogen in ascitic fluid via coagulation and fibrinolysis. In tumor ascites fibrinogen is catabolized to a significantly higher degree via the degradation of crosslinked fibrin. Crosslinked fibrin derivatives may therefore be usable as non-carcinoembryogenic tumor markers.

Ascites↗
PubMed1983

On the aggregation of fibrinogen molecules.

Aggregates of human and bovine fibrinogen were obtained under various conditions, ranging from segment-like precipitates to highly ordered paracrystals and crystals. Their biochemical characterization and the interpretation of their banding pattern by electron optical means was attempted. The observed extra vivum aggregation of fibrinogen without thrombin action, i.e. without cleavage of fibrino-peptides A and B is of particular interest with regard to Copley's theory of the endoendothelial fibrin lining. The in vivo formation of such fibrinogen gels is discussed.

Adenosine Triphosphate↗
PubMed1983

On the aggregation of fibrinogen molecules.

Aggregates of human and bovine fibrinogen were obtained under various conditions, ranging from segment-like precipitates to highly ordered paracrystals and crystals. Their biochemical characterization and the interpretation of their banding pattern by electron optical means was attempted. The observed extra vivum aggregation of fibrinogen without thrombin action, i.e. without cleavage of fibrino-peptides A and B is of particular interest with regard to Copley's theory of the endoendothelial fibrin lining. The in vivo formation of such fibrinogen gels is discussed.

Animals↗
PubMed1975

Antigenic determinants in the disulfide regions of bovine fibrinogen.

Rabbit antibodies to bovine fibrinogen were used to study the antigenic activity of four cyanogen bromide peptides containing the disulfide regions of this molecule. In precipitation tests the highest activity was associated with the peptide F-CB3 which is exclusively derived from the alpha-chain. Reduction of the single disulfide bridge in peptide F-CB3 did not influence its serologic activity. Weaker reactions were observed with the N-terminal multichain peptide F-CB1. The antigenicity of peptide F-CB1 was not affected by removal of fibrinopeptides A and B but it was lost after reduction. The immunological activity of the multichain peptide F-CB2 was even less than that of peptide F-CB1 and the antigenic determinants were destroyed by reduction. A large fragment essentially composed of peptides F-CB1 and F-CB2 could be obtained by limited cyanogen bromide cleavage and showed considerably better immunological activity than peptides F-CB1 and F-CB2 together. Apparently no activity was associated with a mixture of small hydrophobic, disulfide-loop peptides tentatively called peptide F-CB4. The large loss of antigenic activity in cyanogen bromide digests of fibrinogen suggests that the disulfide-stabilized regions do not have an important role in maintaining conformational antigenic determinants of fibroinogen. Changes in noncovalently stabilized conformation requiring uncleaved chains is considered as a possible reason for the findings observed.

Amino Acids↗