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Biomedical subjects

F Watanabe

Publications and source records attributed to F Watanabe.

At least 289 records · Page 16Linked to original sources
PubMed1981

Radioimmunoelectrophoretic analysis of proteins binding 3, 3', 5'-triiodothyronine in human serum.

The binding of purified 131I-3, 3', 5'-triiodothyronine (reverse T3) (rT3) to normal human serum components was investigated by a radioimmunoelectrophoretic technique. When anti-whole human serum was used, five distinct arcs of radioactivity were observed. Evidence was obtained that five of these radioactive arcs were not artifacts, but were due to components binding rT3. From the radioimmunoelectrophoretic patterns with specific antisera, five of these components were identified as thyroxine binding prealbumin, albumin, thyroxine binding globulin (TBG) and alpha 1-and beta-lipoproteins. No radioactive arc of TBG was detected in serum from a patient with TBG deficiency.

Alpha-Globulins↗
PubMed1980

Kinetic investigations on the phase transition of phospholipid bilayers.

Pressure-jump experiments were performed on vesicles and liposomes of dimyristoyl phosphatidylcholine and dipalmitoyl phosphatidylcholine following the time course of solution turbidity. For both lipids two relaxation effects were evaluated the time constants of which exhibit clear maxima at the mid-point of the phase transition. The time constants lie for vesicles in the 100 microseconds and 1 ms ranges and for liposomes in the 1 ms and 10 ms ranges. The processes are slightly faster for dimyristoyl phosphatidylcholine than for dipalmitoyl phosphatidylcholine. All relaxation times are concentration-independent. The time constant and amplitude behaviours indicate that all processes are cooperative in agreement with previous interpretations. It is demonstrated that cooperative units can be evaluated from the relaxation amplitudes. These are of the same order of magnitude as those obtained from static experiments. On the grounds of the present kinetic investigation we can state that the application of the linear Ising model to two-dimensional processes as attempted for the static lipid phase transition is inadequate.

Kinetics↗
PubMed1980

Fluorescence quenching immunoassay of serum cortisol.

Fluorescence quenching immunoassay of serum cortisol was established. The minimal amount of cortisol detected was 3.1 ng/tube and serum concentration of 3.1 micrograms/dl to 100 micrograms/dl of cortisol could be measured. Intra- and inter-assay coefficient of variation were 7.7-10.5% and 10.7-13.3%, respectively. Cortisol values determined by the present method correlated well with those determined by radioimmunoassay (r = 0.97, y = 0.89 x + 0.88, n = 33). This fluorescence quenching immunoassay satisfied the standard criteria of dilution and accuracy, and is a rapid and simple method requiring no antibody-bound and free separation.

Animals↗
PubMed1979

Fluorescence polarization immunoassay for cortisol.

A fluorescence polarization immunoassay for serum cortisol was established using cortisol 21-amine which was readily coupled with fluorescein isothiocyanate. The proposed method is sufficiently sensitive, reliable, specific and simple for routine determination of serum cortisol. The assay is rapid, without separation of antibody-bound and free ligands. The minimal amount of cortisol detected was 1.5 ng/tube and the measurable range was from 1.5 to 100 micrograms/dl. There was a good correlation between values obtained from radioimmunoassay and the proposed method.

Cross Reactions↗
PubMed1979

The analysis of alkaline phosphatase isoenzyme using 4-methylumbelliferyl phosphate as substrate on a cellulose acetate membrane.

A new procedure is established for the analysis of alkaline phosphatase isoenzymes. The electrophoretic separation on cellulose acetate membrane coupled with the detection of alkaline phosphatase activity with 4-methyl-umbelliferyl phosphate as a substrate is described. The proposed method would be useful for the analysis of sample of micro-scale quantities and low activities.

Alkaline Phosphatase↗