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Department of Physiology, Michigan State University, East Lansing 48823
ABSTRACT
The iodinated amino acids of the thyroactive iodinated casein, Protamone, were separated. With two-dimensional thin-layer chromatography, at least 21 iodinated components were demonstrated in the initial n-butanol extract of Protamone hydrolysate. Four of these compounds remained when the alkali-washed hydrolysate was also chromatographed two-dimensionally. Two of these four compounds were identified as thyroxine and triiodothyronine. The concentrations of these two compounds in Protamone were determined to be 0.79 and 0.61%, respectively. The combination of these two values is biologically equivalent in the rat to 3.28% thyroxine. It is concluded that the combined thyroxine and triiodothyronine content of thyroactive iodinated casein is sufficient to account for all of its thyroidal activity in mammals.
1 The data reported herein are taken from a thesis presented by the senior author in partial fulfillment of the requirements for the degree of Doctor of Philosophy, College of Natural Science, Michigan State University, East Lansing. The work was supported in part by NIH Training Grant GM-1121. Michigan Agricultural Experiment Station Journal Article no. 4819.
2 Present address: Department of Physiology, Warner-Lambert Research Institute, Morris Plains, New Jersey.
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