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Biomedical subjects

W Doleschel

Publications and source records attributed to W Doleschel.

At least 19 recordsLinked to original sources
PubMed1988

ATG overdose in a kidney-grafted patient. Clinical course and possible implications.

During antirejection treatment with antithymocyte globulin (ATG), a 48-year-old male kidney graft recipient was erroneously given 30 mg/kg ATG on day 5 of the treatment course. Clinically, the patient presented with abdominal pain, profuse diarrhea, and fever. Initially, the platelet count dropped to 94 x 10(3)/microliters and showed a further decrease to 65 x 10(3)/microliters 2 days thereafter. Plasmapheresis carried out about 12 h after the end of ATG infusion resulted in a decrease in serum levels of total rabbit immunoglobulin as well as the antibody fraction reactive with human T lymphocytes. Within 10 days after the discontinuation of ATG treatment, the relative and absolute number of the T-cell subpopulations, which had disappeared from the circulation at the time of antirejection therapy, returned to normal values. In addition, at this time both platelet and lymphocyte counts were again found to be in the normal range. Kidney function had recovered from the rejection crisis such that the patient could be discharged 26 days posttransplantation.

Antilymphocyte Serum↗
PubMed1982

Specific binding sites on human blood platelets for plasma lipoproteins.

Scatchard analysis of the binding of homologous plasma low density lipoproteins (LDL) to human blood platelets shows the existence of a uniform class of saturable specific binding sites. Platelets from healthy donors bound 1470 +/- 640 molecules of LDL per platelet, the constant of association Ka = (6.2 +/- 2.2) X 10-7 l x mol-1. Binding kinetics, temperature dependence, and experiments with formaldehyde-fixed platelets showed that internalization of LDL (at least the labelled apoprotein moiety) did not occur to any considerable degree under the experimental conditions employed. Both very low density lipoproteins (VLDL) and high density lipoproteins 3 (HDL3) markedly inhibited the binding of LDL. In contrast to LDL, HDL3 bound to 3200 +/- 410 binding sites per platelet with a Ka = (9 +/- 1.7) X 10(7) l x mol-1. Additionally, the results of inhibition experiments using both LDL and HDL3 in combination gave evidence, that the sites for HDL3 binding were not identical with those for LDL binding and each inhibited binding of the other noncompetitively with reduction of the binding affinity and the number of available binding sites. VLDL bound to the platelet plasma membrane in a nonspecific-nonsaturable way. Possible significances of the presence of specific LDL receptors on the platelet plasma membrane for recognized functions of these blood elements are discussed.

Binding, Competitive↗
PubMed1980

[Metabolic indicators ("risk factors") in atherosclerotic coronary heart diseases and the ability to influence these factors by diet].

In view of current interest in the so-called "risk factors" of atherosclerotic cardiovascular diseases and the usefulness of preventive dietary measures, a review is given of the published data from long-term prospective studies. Opinions concerning the importance of the various lipoprotein classes as risk factors and reports of a decrease in the concentration of the allegedly "protective" high-density lipoproteins by consumption of polyunsaturated fatty acids are discussed. An up-to-date summary of current scientific developments relative to this problem is presented.

Cholesterol, Dietary↗
PubMed1980

[Factor VIII preparations of varying purity-examination of physico-chemical parameters (author's transl)].

Commerical preparations of cryoprecipitates, factor VIII concentrates of intermediate purity, and factor VIII concentrates of high purity were studied for their factor VIII related clotting- and platelet-aggregating activities as well as their content of factor VIII antigen. The ratios of the values obtained of these three parameters were used to determine the extent of inactivation of the factor in the preparations. By means of two-dimensional immunelectrophoresis and gel chromatography on Sepharose 4B, the preparations were tested for the presence of atypical factor VIII molecules. Investigations were made to qualify and quantify some of the concomitant proteins in the factor VIII preparations.

Antigens↗
PubMed1979

The influence of thrombin on the platelet-aggregating activity of human factor VIII. A study with insolubilized thrombin.

A study was made of the influence of thrombin on the platelet-aggregating activity of human factor VIII with Ristocetin as cofactor. Purified factor VIII and different amounts of a thrombin-Sepharose 2B complex were mixed and incubated for various periods of time. The factor VIII-related platelet-aggregating activities of the filtrates of the incubation mixtures were determined in a test system using formalin-fixed platelets and Ristocetin as cofactor. The results so obtained indicate that thrombin inactivates the platelet-aggregating activity of factor VIII. The filtrates of the incubation mixtures were also tested by a two-stage test system for the clotting activities. Comparison of the influence of thrombin on the clotting- and the platelet-aggregating activities of factor VIII is presented and discussed.

Animals↗
PubMed1978

The influence of thrombin on the clotting activity of factor VIII. A study with insolubilized thrombin.

An investigation of the influence of thrombin on the clotting activity of factor VIII was made. Purified factor VIII and different amounts of thrombin complexed to Sepharose 4 B were mixed and incubated for various periods of time. The factor VIII activities of these incubation mixtures were determined by the one- and two-stage analytical procedures in the presence of the thrombin-sepharose and in its absence following the latter removal from the test sample by filtration. The results so obtained confirm the view that thrombin inactivates factor VIII. Evidences for a thrombin-induced potentiation of the factor VIII activity, seen only in the thrombin-sepharose containing test samples analyzed by the one-stage method, are here interpreted as thrombin-effects peculiar to this factor VIII test system and not as potentiation by thrombin of the factor itself.

Blood Coagulation↗
PubMed1977

[Lipoprotein analysis by means of the fluorescence probe 8-anilino-1-naphthalene sulphonic acid (author's transl)].

Single and mixed lipoprotein fractions were successfully analyzed by utilizing the fluorescent propertby of the applied reagent, 8-anilino-naphthalene sulphonic acid. The described method is especially useful for determination of lipoproteins present in high dilution, as found in chromatographic column effluents. The concentration dependence of the developed fluorescence was determined and this served as basis for quantitation. Furthermore, the measured activation spectra show two peaks for each lipoprotein class, the relative intesities being different for each class. The intensity quotient shows a tendency towards linear concentration dependence. Investigation of binary and ternary mixtures showed that the ratio of the two maximum intensities is additive, in contrast to the intensities themselves.

Humans↗
PubMed1977

[Separation and stability of australia antigen in human plasma fractions (author's transl)].

Commercially-produced human plasma protein fractions were investigated by a radio-immunological method for their content of Australia antigen (HBsAg). Albumin and gamma globulin solutions in which this antigen was present, were fractionated by isoelectric focussing and gel filtration on Sepharose 4 B. Characterization as to size and electrical charge of the HBsAs was carried out on these preparations. Inactivation studies were performed at different temperatures and concentrations to clarify the question of heat stability of HBsAg in plasma derivates. The importance of additional test methods is discussed.

Chromatography, Gel↗
PubMed1977

[Formation of sub-units of antihaemophilic globulin (factor VIII) by means of high centrifugal force (author's transl)].

The human coagulation factor VIII with a molecular weight greater than 1 X 10(6) Daltons forms active subunits under conditions of high centrifugal force, namely, 200.000 g at 20 degrees C for 32 minutes, as demonstrated by sedimentation analysis. This result was confirmed by Sepharose 4 B gel filtration analysis of the ultracentrifuged product, which revealed, in additon to mateial with a molecular weight of more than 1 X 10(6) Daltons, three F VIII-active fractions with smaller molecular weight values. These observations indicate that these sub-units so produced are not united in the starting matrial by covalent bonds.

Chemical Phenomena↗
PubMed1975

[Isolation of a third human urokinase (S0 type)].

By means of gel diffusion on Sephadex G-150 and isoelectric focusing, a third type of urokinase (S0 type, molecular weight 22,000) was isolated from a commercial urokinase preparation. This urokinase of low molecular weight can be found in the free state or in form of a complex with the S1 type (molecular weight 32,000) thus yielding the S2 type (molecular weight 54,000). By isoelectric fucusing, the latter type can be split into the S0 and S1 types.

Humans↗