An Evaluation of a Plasma Fractionation System^[*)]

Summary

Four primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S_{20, w} and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.

The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S_{20, w} classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

^*) Supported by grant No. H-1108 from the National Institutes of Health. Blood for the large scale fractionation of plasma was obtained from volunteer donors enrolled by the American Red Cross.

^**) Presented in part at the Forty-Third Annual Meeting, Federation of American Societies for Experimental Biology, Atlantic City, April 17, 1959.

^***) In partial fulfillment of the Master of Science degree.

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