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Biomedical subjects

W Stephan

Publications and source records attributed to W Stephan.

At least 127 records · Page 7Linked to original sources
PubMed1979

Anaphylactoid reactions to infusions of plasma protein and human serum albumin. Role of aggregated proteins and of stabilizers added during production.

Six patients suffering from anaphylactoid reactions after infusion of pasteurized plasma (PP) or human serum albumin (HSA) were investigated. Clinical symptoms ranged from urticaria and hypotension to cardiac arrest. Immunoglobulin levels, especially of IgA, were normal, as were concentrations of complement factors C3, C4 and factor B. In skin and lymphocyte transformation tests patients, with the exception of one severely allergic to protein, did not react to the monomeric pure HSA. Five out of six patients reacted against HSA aggregates and three patients to the HSA modified by caprylate added as stabilizer during commercial HSA production. It is concluded that the anaphylactoid reactions developing after PP or HSA infusion result from a non-specific reaction to protein aggregates and in some cases possibly from a specific immune response to the caprylate-modified HSA.

Anaphylaxis↗
PubMed1978

Elimination and organ distribution of intravenously administered allogeneic and xenogeneic IgG modifications. (Standard IgG, F (ab)2-fragments and beta-propiolactone treated IgG) in dogs.

Dog IgG was produced by fractionation procedures used for the production of clinically used i.v. gammaglobulins. Chemical modification of dog IgG was done by pepsin or beta-propiolactone treatment. The intravascular half-life of beta-propiolactone IgG was 8.5 +/- 2.1 days compared to 4.5 +/- 1.6 days of pepsin treated IgG. Tissue concentrations of radioactive labelled beta-propiolactone IgG were generally higher than of pepsin digested IgG. Pepsin treated Igg was degraded to a significantly higher extent (26% of the administered radioactivity was bound to fragments smaller than 6000 MW after three days) than beta-propiolactone IgG (9% fragments after the same interval, P less than 0.001). It is concluded that the short intravascular half-life of pepsin IgG cannot be explained by increased extravascular filling, but is due to rapid degradation and excretion via the kidneys. There was no obvious difference in elimination and organ distribution between standard and beta-propiolactone IgG.

Animals↗
PubMed1978

Altered metabolism of phospholipids in the lung of rats with peritonitis.

Pulmonary alterations after shock and sepsis, described clinically as shock lung or adult respiratory distress syndrome, are of great importance in intensive care. Pathogenetically an alteration of the surfactant system of the lung is often discussed. Since phospholipids are constituents of lung surfactants, phospholipid metabolism is investigated in experimental peritonitis in rats in our laboratory. 15 hours after inducing a peritonitis, the lung incorporates more oleic acid than that in animals of the reference group. 33 hours after inducing peritonitis, the capacity of the lung to incorporate choline and fatty acids is markedly reduced, histologically the lungs represent morphological equivalents of the so-called shock lung at this time. Therefore we conclude, that an alteration of phospholipid metabolism with a diminished and/or altered synthesis of lung surfactant plays, at least in part, an important role in the pathogenesis of respiratory distress in sepsis and peritonitis.

Animals↗
PubMed1977

[Concentration of intravenously administered gammaglobulin preparations in dog skin (author's transl)].

Chemical modification of standard gammaglobulin with enzyme treatment (pepsin) or stabilization (beta-propiolactone) is able to influence elimination, fragmentation and organ distribution of intravenously administered gammaglobulins as shown in 36 dogs after i.v. application of allogenic and xenogenic gammaglobulin preparations. Pepsin-gammaglobulin was eliminated and fragmented most rapidly. Gammaglobulin concentrations of all preparations in the skin showed as slower decrease than comparable blood concentrations. The highest skin concentrations 10 days after i.v. application were found for beta-propiolactone gammaglobulin with 6.2 +/- 1.6 microgram/g compared to a blood level of 7.9 +/- 0.9 microgram/ml.

Animals↗
PubMed1976

[Prevention of HBs antigen-positive serum hepatitis with hyperimmune-globulin anti-HBs].

Selection of donors to prevent HBs-antigen positive serum hepatitis has been only partially successful. For this reason the attempt was made to prevent the disease by passive immunisation with anti-HBs antibodies. A prerequisite for the systematic use of such immunisation is the determination of antibody threshold which would still provide protection. Plasma elimination of transmitted. HBs antibodies was serially measured in five children with terminal renal failure and ten normal subjects after intensive contact with HBs antibodies. Half-life values indicated marked individual variations which have to be taken into account with long-term prophylaxis. In the children they were 28.5, 25.9, 16.6, 11.7 and 7.8 days, respectively. In the healthy subjects the half-life averaged 20.3 days. The long-term programme developed by the authors appears to be suitable for revealing the value of hyperimmune-globulin anti-HBs in the prevention of HBs-antigen positive serum hepatitis.

Antibodies, Viral↗
PubMed1976

Gas chromatographic trace analysis of beta-propiolactone in sterilized serum proteins.

A method for detecting traces of beta-propiolactone, which was previously described by Schmitz-Masse, has been modified and adapted to the analysis of protein solutions. Using this method, the rate of hydrolysis of beta-propiolactone (beta-P1) was examined and beta-P1 sterilized commercial products were analyzed for possible residual nonhydrolyzed beta-P1.

Blood Proteins↗
PubMed1975

Undegraded human immunoglobulin for intravenous use.

A report is presented on the development and the properties of a nondegraded human immunoglobulin preparation suitable for intravenous administration. Intravenous tolerance is achieved by elimination of anticomplementary activity through modification with beta-propiolactone. The natural antibody characteristics, such as antibody activity, molecular weight, and half-life, are retained. The findings presented open up new perspectives for an extension of the range of indication for intravenous immunoglobulin.

Adsorption↗