THYROXINE-BINDING PROTEINS IN THE SERUM OF THE GREY KANGAROO

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Abstract
Species differences have been described in the thyroxine-serum protein complexes of various mammals (Blumberg & Robbins, 1960; Farer, Robbins, Blumberg & Rail, 1962; Rösler, 1967a, b). The thyroid hormone-binding serum proteins of the pouched mammals have not been studied. Because this order (Marsupialia) has had a long separate evolutionary history, its protein patterns are of interest and have been used to study speciation (Kirsch & Poole, 1967). We report here electrophoretic studies of the binding of thyroid hormones by serum proteins of the grey kangaroo. Sera were obtained from Eastern (Macropus giganteus) and Western (Macropus fuliginosus) grey kangaroos and from a hybrid (Eastern x Western) maintained by the Division of Wildlife Research, C.S.I.R.O. Except for one Western specimen, all sera were from adult females. Sera were labelled with 0·9–2·4 μg. [131I]thyroxine (T4)/100 ml. or 0·9–1·4 μg. [125I]tri-iodothyronine (T3)/100 ml. obtained from Abbott Laboratories (North Chicago,

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