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1 Radioisotope Service, Veterans Administration Hospital, and Department of Medicine, University of Oklahoma School of Medicine, Oklahoma City, Oklahoma
Calcium-45 binding by human albumin and prealbumin has been studied. Protein separation was performed by continuous paper electrophoresis. Calcium-45 was added to the fractions and the mixture incubated at 37°C for 24 hours. Unbound calcium-45 was removed by dialysis against tap water for 16 hours, the pH of the fractions remained between 8.69.1 at all times. Aliquots of the fractions were then counted with a micromil gas flow counter. The greatest specific activity was found in several tubes preceding the albumin, i.e. with faster electrophoretic mobility than classical albumin. The calcium-binding ability of this fraction, which has been previously called prealbumin, exceeded that of classical albumin by sixfold.
Submitted on December 1, 1958
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