EFFECTS OF PHYSICOCHEMICAL AGENTS ON THE ELECTROPHORETIC PROPERTIES OF SERUM PROTEINS IN STARCH GEL MEDIUM

The effects of physical and chemical agents on the electrophoretic properties of the serum proteins have been investigated utilizing both starch gel and paper electrophoresis. It has been found that freezing and thawing do not produce any alterations in the serum proteins whereas heating at either 47 °C or 55 °C causes a certain degree of homogenization of the serum proteins.

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EFFECTS OF PHYSICOCHEMICAL AGENTS ON THE ELECTROPHORETIC PROPERTIES OF SERUM PROTEINS IN STARCH GEL MEDIUM

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o62-006 ◽

1962 ◽

Vol 40 (1) ◽

pp. 35-39

Author(s):

M. Richter ◽

J. Gold ◽

W. Rankowicz ◽

B. Rose

Keyword(s):

Serum Proteins ◽

Paper Electrophoresis ◽

Freezing And Thawing ◽

Chemical Agents ◽

Starch Gel ◽

Physical And Chemical

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Bovine Platelet Proteins II. Purification of Platelet Fibrinogen

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653556 ◽

1969 ◽

Vol 21 (03) ◽

pp. 419-427 ◽

Cited By ~ 5

Author(s):

N. O Solum ◽

S Łopaciuk

Keyword(s):

Analytical Ultracentrifugation ◽

Insoluble Fraction ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Starch Gel Electrophoresis ◽

Freezing And Thawing ◽

Insoluble Material ◽

High Resolution Power ◽

Starch Gel ◽

Platelet Proteins

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.

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