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Biomedical subjects

W Hertl

Publications and source records attributed to W Hertl.

9 recordsLinked to original sources
PubMed1987

A differential pulse polarographic serum protein assay.

Human serum and albumin show a differential pulse polarographic band near -0.6 V. For sufficiently dilute solutions (less than 7 micrograms/ml) at pH 7.0, the polarographic response is linearly related to the solution concentration. At pH 12.6 a near-linear response to 70 micrograms/ml is obtained, but sample equilibration time is slow. The polarographic assay for total serum protein using bovine serum albumin (BSA) to generate a standard curve gave a correlation coefficient of 0.89. The cellular constituents of whole blood do not interfere. The correlation with BSA does not hold for protease-digested serum or albumin.

Adsorption↗
PubMed1984

Assessment of cell-substrate adhesion by a centrifugal method.

A centrifugal method has been evaluated for measuring the strength of Vero Green Monkey kidney cell adhesion to growth surfaces. The centrifugal force necessary to remove cells gave a quantitative measure of cell adhesion and hence the quality of the growth surface. After being subjected to high gravity forces, both the remaining attached cells and the detached cells were viable, indicating the detachment process did not simply rupture the cell. Electron microscope examination of growth surfaces after cell detachment suggested that remnants related to filopodia remained.

Animals↗
PubMed1984

Surface treatments and cell attachment.

Photoelectron spectroscopic examination of treated plastic surfaces showed that surface oxidation, primarily as carboxyl groups, was responsible for formation of good growth surfaces. Gas-plasma studies indicated that only very short exposures were required and that the effect was confined to a thin surface layer that produced adhesive surfaces. Highly adhesive surfaces were produced using oxidizing chemicals. Studies with a polymeric ester demonstrated the importance of unesterified carboxyl groups for high adhesiveness.

Animals↗
PubMed1982

Enzyme immunoassay for free thyroxin.

We describe a mathematical model for a single-tube enzyme immunoassay for free thyroxin (FT4), involving use of a thyroxin/horseradish peroxidase (EC 1.11.1.7) conjugate that does not interact with thyroxin-binding globulin. In the presence of serum two populations of unassociated, or free, immunologically active constituents are present: FT4 and the conjugate. The concentrations of the former are determined by the serum constituents and of the latter by the albumin concentration. When a small quantity of antibody is added, it reacts with the variable amount of FT4 and with the constant amount of the conjugate, thus giving a measure of the FT4. We constructed a mathematical model based on thermodynamic binding constants and adsorption data. The model gives satisfactory agreement with the experimental data under a variety of experimental conditions. Results for 19 patients' serum samples demonstrate the validity of the concept.

Horseradish Peroxidase↗