The thyroxine-serum protein complexes have been studied by means of electrophoresis at pH 8.6 using starch gel and paper as a supporting medium. Borate buffer was used in the gel experiments and barbital or ammonium carbonate in the paper experiments. On gel electrophoresis, most humans bind thyroxine in and near the albumin zone. Band 1 corresponds to the fastest moving prealbumin, Band 2 is at the leading edge of the broad albumin zone, band 3 is diffuse and located in the slowest half of the albumin zone and Band 4 travels immediately behind the albumin. Monkeys have a pattern similar to humans but there is a variation in the position of Band 1 and in the fastest moving prealbumin protein which may constitute a polymorphic system. Concomitant variation was found in the mobility of the prealbumin thyroxine complex (TBPA) in paper electrophoresis in ammonium carbonate. In the cow, both Band 1 and TBPA appear to be absent, and other thjTOxine-protein bands in starch gel electrophoresis are found which hav...
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Blumberg et al. (1960) studied this question.