Studies in bisalbuminemia: binding properties of the two albumins.

By EDWARD J. SARCIONE AND C. WILLIAM AUNGST H UMAN PLASMA PROTEINS are known to vary both qualitatively and quantitatively from the normal in various acquired disease states. In addition, genetic alterations in plasma proteins of man are known; these have been summarized by Gitlin and Janeway.2 The present study resulted from the finding of a markedly abnormal serum protein pattern in a patient with Wegener’s granulomatosis. On paper electrophoresis, this was characterized by a large increase in a component with a mobility similar to a1-globulin and a concomitant decrease in the albumin fraction. This resembled the electrophoretic pattern described in the rare genetic defect, bisalbuminemia. In order to determine whether this finding represented a dysproteinemia characteristic of Wegener’s granulomatosis or was indeed another instance of bisalbuminemia, detailed studies of the patient’s serum and sera of his relatives were performed. The anomalous protein pattern in this subject and five members of his family was identified as bisalbuminemia; hence an additional family having this rare defect is available for study. In the course of attempts to characterize the two albumins in sera of affected members of the family, differences in their relative abilities to bind added P31-thyroxine were detected.