Search PubMed⌕ Search

Biomedical subjects

S Baudner

Publications and source records attributed to S Baudner.

33 records · Page 2Linked to original sources
PubMed1981

[Isolation and crystallization of the Clr subunit of the first component of human complement (author's transl)].

Isolation of Clr from Cohn-Fraction I of human plasma is accomplished by a series of steps which include affinity chromatography on IgG-p-azobenzyloxyethylsulfonylethoxy-Sepharose CL-4B, ion exchange chromatography and preparative zone electrophoresis. The protein is easily soluble in 0.1 M Tris/HCl buffer, pH 10.0 and is crystallized readily by means of dialysis against 0.15 M saline, pH 7.0 in the form of hexagonal dipyramides. The structural elucidation using X-ray analysis is now possible.

Chromatography, Affinity↗
PubMed1981

Determination of tiamenidine in biological specimens by radioimmunoassay.

A simple and highly sensitive radioimmunoassay (RIA) procedure has been developed for the determination of the new antihypertensive drug 2-[(2-chloro-4-methyl-3-thienyl)amino]-2-imidazoline (tiamenidine) in serum, plasma and urine. Antisera to tiamenidine were produced in rabbits against its derivatives conjugated to bovine serum albumin. Studies with metabolites and imidazoline derivatives have shown that the antibodies thus produced are specific for tiamenidine. 3H-Labelled drug was used as tracer. The separation of free from antibody-bound tiamenidine was carried out by using polyethylene glycol. The radioimmunoassay (RIA) allows the determination of tiamenidine in 100 microliter biological specimens directly and without extraction down to a detection limit of 20 pg/ml. Reproducibility and accuracy of the assay are good. A sufficient correlation (r = 0.95) was obtained when serum samples were assayed by the RIA and the GC-MS method. The pharmacokinetic profile of the drug was determined in subjects after oral administration of 1 mg tiamenidine using the newly developed RIA. The course of serum levels up to 24 h after treatment may be well described by a Bateman function with an elimination half-life of about 3-5 h. These values correspond sufficiently well with the data obtained from the rate constant of the excretion via urine.

Animals↗
PubMed1979

A new method for fluorescence immunoassay using plane surface solid phases (FIAPS).

A method distinguished by high sensitivity, low non-specific binding, easy handling, and broad applicability with respect to various antigens is described. Films of polymethyl-methacrylate with plane surfaces were selected as solid phase for adhesive or covalent binding of different antigens (DNA, histone, human, rabbit or goat immunoglobulins). Proteins were covalently bound to the films by the azide method (Orth and Brummer, 1972). Polymethylmethacrylate films thus coated had a negligible autofluorescence and gave minimal non-specific binding of protein. Coated films were used for specificity control of FITC-labeled antibody preparations and in the double antibody and sandwich techniques for detection of antibodies or antigens in sera from man, rabbit and goat. FITC-conjugated hyperimmune antibody, in some cases purified by immunoadsorption was used as second antibody in indirect techniques. The amount of fluorescent-labeled antibody bound per unit of surface area of film was measured by incident light with a Zeiss-Axiomat fluorescence microscope equipped for fluorescence photometry and an uranyl acetate glass plate was used as a standard. The technique appears superior to present methods of quantitative immunofluorescence analysis.

Animals↗
PubMed1977

Determination of nomifensine by a sensitive radioimmunoassay.

1. A radioimmunoassay (RIA) has been developed for determination of both nomifensine and total nomifensine (nomifensine + conjugated nomifensine) in serum, plasma, and urine. 2. Antibodies were prepared in rabbits by immunization with N-(8-Nomifensine) succinamic acid-bovine serum albumin. 3H-labelled drug was used as tracer. Separation of free from antibody-bound nomifensine was carried out using dextran-coated charcoal. For determination of total nomifensine, the acid-labile conjugate was split by acidification. 3. The limit of detection for nomifensine is 300 pg/ml plasma and the cross-reactivity of the metabolites is less that 1%. The influence of conjugated nomifensine on the results of nomifensine can be corrected. 4. Pharmacokinetics of nomifensine were determined in healthy volunteers after oral administration of 100 mg 14C-labelled drug. Peak levels of 14C radioactivity (2,150 ng/ml), total nomifensine (1,252 ng/ml) and nomifensine (53 ng/ml) appeared within 1.5-2 h; the half-life of elimination from plasma was 1.5-2 hours. The advantages of this routine method are high sensitivity, the requirement of small amounts of plasma, and simple handling.

Administration, Oral↗
PubMed1977

[Isolation and characterization of an unknown, leucine-rich 3.1-S-alpha2-glycoprotein from human serum (author's transl)].

This article describes the isolation and characterization of a previously unknown, leucine-rich 3.1S-alpha2-glycoprotein from human serum. The starting material was Supernatant II, which is a byproduct in the large-scale preparation of albumin and gamma-globulin by the ethacridine lactate/ammonium sulfate procedure. The purified protein is homogenous both in carrier-free and molecular-sieve electrophoresis. Its electrophoretic mobility indicates that it belongs to the alpha2-globulins. Isoelectric focussing splits it into 4 bands with isoelectric points between 3.8 and 4.1. In the ultracentrifuge it sediments in a single band at 3.1S. The molecular weight determined by equilibrium sedimentation is 49 600 +/- 4 000. Subunits were not detected. Chemical analysis reveals it to be a glycoprotein with a carbohydrate content of 23%. The amino acid content is unusual in that the leucine content is almost 17%, i.e. about every fifth amino acid is a leucine. The average concentration of the leucine-rich 3.1S-alpha2-glycoprotein in human serum was determined by a quantitative immunological method as 2.1 mg per 100 ml. The protein is not related to any of the previously known well characterized serum proteins.

Alpha-Globulins↗
PubMed1975

[Isolation of beta2-microglobulin from human colostrum (author's transl)].

The beta2-microglobulin from human colostrum was purified by a combination of ordinary protein-chemical techniques: gel filtration, ion-exchange chromatography and zone electrophoresis. The procedure is organized in such a way that the simultaneous isolation of many other milk proteins is possible. The beta2-microglobulin obtained from colostrum cannot be distinguished by physical-chemical or immunological means from the beta2-microblobulin isolated from the urine of patients with kidney-tubule diseases. At the beginning of lactation, human milk contains significantly more than 10 mg/-100 ml beta2-microglobulin, but the concentration drops within two or three days to 15-30% of the original amount.

Beta-Globulins↗