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Clinical Chemistry 1: 253-263, 1955;
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Clinical Chemistry, Vol 1, 253-263, Copyright © 1955 by the American Association for Clinical Chemistry

Serum Beta-Lipoproteins of Normal,Atherosclerotic, and Lipemic Individuals

Changes in Concentration, Stability, and Mobility upon Incubati at 6.5° and 37.5°, as Determined by Paper Electrophoresis

Sidney P. Gottfried 1, Russell H. Pope 1, Nathan H. Friedman 1, Irving B. Akerson 1, and Salvatore Di Mauro 1

1 Biochemistry, Pathology, and Medical Departments of Bridgeport Hospital Bridgeport, Conn.

1. Serum lipids, cholesterol, and lipoproteins were determined on 8 normal 7 atherosclerotic, and 8 lipemic individuals in the fasting state. Serum lipids and cholesterol were determined chemically, the lipoprothins by paper electrophoresis. Serum lipoproteins were also performed after incubating at 6.5° and 37° for 24, 48, and 72 hours, and changes in the physical appearance of the serum, and in the concentration and mobility of the beta-lipoproteins were observed. In 12 of the above cases, serum protein patterns were noted with the lipoprotein patterns.

2. In many cases a visible turbidity appeared upon incubating at 37°, never upon incubating at 6.5°. Inmost cases this turbidity appeared after incubating for 48 hours, and tended to occur more frequently in atherosclerotic sera than in normal sera.

3. The concentration of beta-lipoproteins decreased upon incubating either at 6.5°orat 37°, the decrease being of the same order of magnitude for normal, atherosclerotic, or lipemic sera.

4. Incubating at 37°increased the mobility of the beta-lipoproteins (except when a turbidity appeared), the peak shifting from between the beta- and gamma-globulins to between the beta- and gamma-globulins. Incubating at 6.5° had no effect on the mobility of the beta-lipoprotein.

5. When a turbidity appeared upon incubating at 37°, the mobility of the beta-lipoproteins decreased, the peak shifting toward the origin. As the turbidity became marked, a sixth protein fraction appeared, of slower mobility than the gamma-globulin. This protein fraction first appeared to form at the expense of the beta- and gamma-globulins and then at the expense of the alpha-globulins, all of which decreased. It is considered that the turbidity is due to the formation of "denatured" proteins and lipoproteins which are characterized by a decrease in mobility.

6. No consistent changes were noted in the concentration, stability and mobility of the alpha-lipoproteins upon incubating at either 6.5° or 37°.

Submitted on February 4, 1955







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Copyright © 1955 by the American Association for Clinical Chemistry.