Thyroxine stimulation of amino acid incorporation into protein.
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Biomedical subjects
Publications and source records attributed to S KAUFMAN.
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The effect of thyroxin on the in vitro incorporation of dl-leucine-l-C(14) into the protein of rat liver homogenates has been investigated. Both thyroxin pretreatment in vivo and thyroxin in vitro at a concentration of 1 x 10(-5) M were found to increase the rate of amino acid incorporation. The increased activity following the thyroxin pretreatment in vivo was found to be localized in the mitochondrial fraction. It is suggested that the acceleration of metabolic rate characteristic of thyroxin action may be secondary to the stimulation of energy-requiring reactions such as protein synthesis.
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The enzymatic conversion of phenylalanine to tyrosine had previously been shown to require a nonprotein cofactor. It has now been demonstrated by direct assay that the cofactor is present in phenylketonuric liver samples. The lack of a functional phenylalanine hydroxylating system in phenylketonuria is not due to the absence of the cofactor.
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