STUDY OF VIRAL ANTIBODIES BY THE PAPER-RADIOACTIVE VIRUS METHOD

PEDIATRICS ◽  
1966 ◽  
Vol 37 (1) ◽  
pp. 7-18
Author(s):  
Horace L. Hodes ◽  
Ruth Berger ◽  
Eugene Ainbender ◽  
Helen D. Zepp ◽  
Maria M. Hevizy

1. A filter paper-radioactive virus method for the detection and study of viral antibodies in human serum is described. The method gives accurate and reproducible results. It is particularly suitable for antibody testing on a mass basis. A slight modification makes the method more sensitive than standard tissue culture neutralization tests. 2. The major poliovirus antibody in human serum combines with the virus to form a particle which is non-infectious and of low mobility.

1956 ◽  
Vol 2 (3) ◽  
pp. 145-159 ◽  
Author(s):  
Joseph T Anderson ◽  
Ancel Keys

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.


Biomedicines ◽  
2020 ◽  
Vol 8 (7) ◽  
pp. 209 ◽  
Author(s):  
Lulu Wu ◽  
Athanasios Mantas ◽  
Simon Gustafsson ◽  
Levon Manukyan ◽  
Albert Mihranyan

This study is dedicated to the rapid removal of protein aggregates and viruses from plasma-derived human serum albumin (HSA) product to reduce the risk of viral contamination and increase biosafety. A two-step filtration approach was implemented to first remove HSA aggregates and then achieve high model virus clearance using a nanocellulose-based filter paper of different thicknesses, i.e., 11 μm (prefilter) and 22 μm (virus filter) at pH 7.4 and room temperature. The pore size distribution of these filters was characterized by nitrogen gas sorption analysis. Dynamic light scattering (DLS) and size-exclusion high performance liquid chromatography (SE-HPLC) were performed to analyze the presence of HSA aggregates in process intermediates. The virus filter showed high clearance of a small-size model virus, i.e., log10 reduction value (LRV) > 5, when operated at 3 and 5 bar, but a distinct decrease in LRV was detected at 1 bar, i.e., LRV 2.65–3.75. The throughput of HSA was also dependent on applied transmembrane pressure as was seen by Vmax values of 110 ± 2.5 L m−2 and 63.6 ± 5.8 L m−2 at 3 bar and 5 bar, respectively. Protein loss was low, i.e., recovery > 90%. A distribution of pore sizes between 40 nm and 60 nm, which was present in the prefilter and absent in the virus filter, played a crucial part in removing the HSA aggregates and minimizing the risk of virus filter fouling. The presented results enable the application of virus removal nanofiltration of HSA in bioprocessing as an alternative to virus inactivation methods based, e.g., on heat treatment.


1958 ◽  
Vol 36 (1) ◽  
pp. 1159-1166 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon

The biocolloids of normal urine have been isolated and characterized by free electrophoresis and electrophoresis on filter paper. An average of 133 mg of material was recovered from 24-hour aliquots of normal urine. This material was composed of at least seven components as revealed by free electrophoresis at pH 8.6. Five of these components were similar in electrophoretic mobility to the five serum components. A relatively large amount of material was present which behaved like the acid mucoproteins of normal serum. No lipoproteins were detected. Some of the components of the urinary biocolloids were shown to be derived from human serum γ-globulins by labelling the latter with radioactive iodine.


1994 ◽  
Vol 77 (3) ◽  
pp. 758-760
Author(s):  
Ugo R Cieri

Abstract A procedure is presented for the determination of reserpine in tablets by liquid chromatography (LC) that is a slight modification of a method presented in a previous publication. The sample is extracted with methanol, and solutions are filtered through filter paper. For LC, a 7.5 cm column is used; the mobile phase is methanol containing a small volume of an aqueous solution of the sodium salt of 1-pentanesulfonic acid. Detection is by fluorescence with 280 nm excitation and 360 nm emission. Two commercial samples containing 0.1 and 0.25 mg reserpine were analyzed. For each sample, 2 determinations were made on a ground composite. Ten tablets were also analyzed individually. A linearity study was conducted, with solutions ranging in concentration from 80 to 120% of the amount present in the reference solution.


1984 ◽  
Vol 15 (6) ◽  
pp. 575-580 ◽  
Author(s):  
Donald H. Silberberg ◽  
Margaret C. Manning ◽  
Alan D. Schreiber

1957 ◽  
Vol 3 (6) ◽  
pp. 813-819 ◽  
Author(s):  
F. L. M. Turel ◽  
G. A. Ledingham

Dense, felt-like growth of aerial mycelium of Melampsora lini (Pers.) Lév. was obtained when surface-sterilized, rust-infected cotyledons of flax were put on a modified Knop medium, containing fresh, ripe coconut milk, sucrose, and Difco Bacto-Agar. The mycelium remained fully dependent on the living host tissue, but could easily be collected free from host material in quantities sufficient for respiration and small scale chemical studies. Slight modification of the method allowed production of appreciable quantities of uredospores free from contaminating microorganisms.


1978 ◽  
Vol 119 (6) ◽  
pp. 777-779 ◽  
Author(s):  
Michel Boileau ◽  
Edward Keenan ◽  
Elaine Kemp ◽  
Russell Lawson ◽  
C.V. Hodges

Diabetes ◽  
1987 ◽  
Vol 36 (12) ◽  
pp. 1401-1407 ◽  
Author(s):  
S. Sandler ◽  
A. Andersson ◽  
A. S. Landstrom ◽  
J. Tollemar ◽  
H. Borg ◽  
...  

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