scholarly journals Studies on Donaggio Reaction Positive Substance and Akamatsu-Shinmei Reaction Positive Substance in Human Serum by means of Filter-Paper Electrophoresis

1958 ◽  
Vol 13 (2) ◽  
pp. 188-193
Author(s):  
Masana Ogata ◽  
Yoshio Mochizuki
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.


Science ◽  
1952 ◽  
Vol 115 (2997) ◽  
pp. 626-627 ◽  
Author(s):  
F. Larson ◽  
W. P. Deiss ◽  
E. C. Albright

1954 ◽  
Vol 3 (4) ◽  
pp. 263-269 ◽  
Author(s):  
IAN R. MACKAY ◽  
WADE VOLWILER

1954 ◽  
Vol 32 (1) ◽  
pp. 567-570
Author(s):  
S. D. Vesselinovitch ◽  
H. S. Funnell

A technique for filter paper electrophoresis and strip staining that permits the running time to be reduced to two hours or less is described. Some typical two hour electrophoretic patterns are illustrated and the clinical advantages of the technique mentioned. Details of a simple and inexpensive apparatus for electrophoresis on filter paper are given. Several variables affecting rapid and distinct protein separation, which were modified in the development of this method, and the relationships between these changes and the shortened running time are discussed.


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.


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