A New Haemoglobin Variant Haemoglobin J Birmingham a 120 (H3) Ala → Glu

An abnormal haemoglobin, which on paper electrophoresis has the mobility of Hb J, has been found in two brothers and, in the heterozygous state at least, is not associated with serious clinical abnormality. The structure of this hitherto unreported haemoglobin is α 120 (H3) Ala → Glu and it is named Haemoglobin J Birmingham.

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METHODOLOGICAL STUDY OF THE RADIOIMMUNOASSAY OF HUMAN THYROTROPHIN

Acta Endocrinologica ◽

10.1530/acta.0.0710024 ◽

1972 ◽

Vol 71 (1) ◽

pp. 24-36 ◽

Cited By ~ 24

Author(s):

Ariel Gordin ◽

Pirkko Saarinen

Keyword(s):

Healthy Subjects ◽

Binding Capacity ◽

Paper Electrophoresis ◽

Storage Conditions ◽

Methodological Study ◽

Double Antibody ◽

The Mean ◽

Specific Activities ◽

Initial Binding ◽

In Pregnancy

ABSTRACT An account is given of a methodological study of the double-antibody radioimmunoassay of human TSH, using highly purified labelled human TSH as tracer. It was shown that conventional paper electrophoresis was not adequate for studying the purity of labelled human TSH. When polyvinylchloride (Pevikon®) electrophoresis was used, four subfractions could still be separated, even though, on paper electrophoresis, the material seemed to be homogeneous. Only two of the four Pevikon fractions were immunoreactive. Purification of labelled human TSH by Pevikon electrophoresis also improved the sensitivity of the assay. Specific activities of about 100 mCi/mg gave the highest initial binding capacity, produced least damage to the labelled hormone and showed the best stability of the tracer without influencing the sensitivity of the method. In different storage conditions, labelled human TSH was found to be most stable at −20°C and diluted 1/100. Only in pregnancy did the addition of HCG seem necessary. The mean TSH value in healthy subjects was 3.6 ± 1.4 μU/ml (mean±sd) with a range from 1.6 μU/ml to 8.8 μU/ml.

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Improved Separation of Serum Proteins in Paper Electrophoresis - A New Electrophoresis Buffer

Scandinavian Journal of Clinical and Laboratory Investigation ◽

10.3109/00365515709079983 ◽

1957 ◽

Vol 9 (4) ◽

pp. 338-341 ◽

Cited By ~ 3

Author(s):

T. Aronsson ◽

A. Grönwall

Keyword(s):

Serum Proteins ◽

Paper Electrophoresis

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Automatic paper electrophoresis

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19620969 ◽

1962 ◽

Vol 27 (4) ◽

pp. 969-973 ◽

Cited By ~ 1

Author(s):

J. Hrdina ◽

M. Pechman ◽

J. Škoda

Keyword(s):

Paper Electrophoresis

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Macroglobulinemia: The Usefulness of DL-Penicillamine and Paper Electrophoresis in Diagnosis

Clinical Chemistry ◽

10.1093/clinchem/10.7.600 ◽

1964 ◽

Vol 10 (7) ◽

pp. 600-605 ◽

Cited By ~ 2

Author(s):

Donald J Campbell ◽

Thomas Boenisch

Keyword(s):

Paper Electrophoresis ◽

Myeloma Protein

Abstract The change in mobility of an abnormal globulin peak during paper electrophoresis in the presence of DL-penicillamine is the most useful of simple procedures suggested for differentiation between macroglobulin and myeloma protein. However, not all cases indicating macroglobulin by this procedure will correlate with criteria based on ultracentrifuge analysis or antigenic reaction.

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Cholesterol in Serum and Lipoprotein Fractions

Clinical Chemistry ◽

10.1093/clinchem/2.3.145 ◽

1956 ◽

Vol 2 (3) ◽

pp. 145-159 ◽

Cited By ~ 187

Author(s):

Joseph T Anderson ◽

Ancel Keys

Keyword(s):

Human Serum ◽

Total Cholesterol ◽

Filter Paper ◽

Room Temperature ◽

Paper Electrophoresis ◽

Cholesterol Content ◽

Intraindividual Variability ◽

Detailed Data ◽

The Stability ◽

Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

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