Sulphate and glucuronide conjugation of cortisol in the normal human, cataractous, bovine, rabbit and rat lens in vitro have been investigated using a cortisol-4–14C. The authors have verified the presence of sulphate and glucuronide conjugation of cortisol in the lens. There are species differences in conjugation of steroid in the lens. Conjugation in the human lens was found to be more active than that in other animals. Sulphate conjugation of cortisol in the cataractous lens was less than that in a normal human lens, whereas no change was found in glucuronide conjugation. These results have demonstrated that the lens is one of the organswhich conjugate the steroid hormone actively.
The authors have found that cysteine markedly increased the cortisol-binding capacity of the lens in vitro and that the oxidized form of glutathione acted as an inhibitor on the cortisol-binding capacity in the lens. The effect of exogenous sulphydryl group, especially cysteine, may have resulted from activation of endogenous sulphydryl groups as a bindingsite for cortisol.
The distribution rate of sodium iodide (Na131I) and toxohormone labeled with Na131I in rats under various experimental conditions was described. Toxohormone extracted from the cancer tissue of the stomach removed by surgical operation exhibited a remarkable inhibitory effect on liver catalase. Compared with the distribution of Na131I in the liver and spleen of the normal rats, that of Na131I labeled toxohormone in the above organs was found to be characteristically decreased. It was also decreased in the liver of splenectomized rats. The distribution of Na131I was reduced in the liver and spleen of rats, which had been treated with toxohormone for successive two days. It was also decreased in the above organs of rats with moderate liver impairment.
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