Iodide goiter and the pharmacologic effects of excess iodide.
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Biomedical subjects
Publications and source records attributed to J Wolff.
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Dimethyl sulfoxide inhibits horse liver alcohol dehydrogenase. In the direction of aldehyde reduction, this inhibition is competitive with aldehyde, with an inhibition constant of 5 x 10(-3)M. Dimethyl sulfoxide reacts with the binary complex consisting of enzyme and the reduced form of nicotinamide -adenine dinucleotide to form a highly fluorescent ternary complex, with a dissociation constant similar to the inhibition constant. The inhibition of aldehyde reduction can be interpreted as due to competition between aldehyde and dimethyl sulfoxide for the carbonyl binding site of the above-mentioned binary complex.
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Accumulation of iodide by thyroid tissue is inhibited by two phospholipase A-free proteins from cobra venom, filipin, crude phospholipase C, and lysolecithin. The venom proteins decrease K(+) in tissue but do not significantly affect incorporation of phosphorus-32 into phospholipid or stimulation of this process by thyrotropin. However, filipin and crude phospholipase C, like thyrotropin, do increase phospholipid formation.
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