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Citation Information: J Clin Invest. 1976;58(3):551-556. https://doi.org/10.1172/JCI108500.
Abstract
Frozen liver tissue from an individual identified several years ago as sulfite oxidase deficient has been reexamined in light of new knowledge which has been obtained regarding the enzyme. It has been established that hepatic molybdenum levels and xanthine oxidase activity were within normal values and comparable to those observed in control samples preserved from the original study along with the deficient tissue sample. The ability of the patient's liver to synthesize the specific molybdenum cofactor required for activation of de-molybdo sulfite oxidase also appears to have been unimpaired. Using an antibody preparation directed against rat liver sulfite oxidase which also inhibits and precipitates the human enzyme, it has been determined that cross-reacting material with determinants recognized by inhibiting antibodies is absent in the liver sample from the deficient patient. Immunodiffusion experiments gave strong precipitin bands against the control liver extracts, but showed no detectable precipitin reaction between the deficient liver extract and the antibody preparation. The relationship of these findings to a second patient recently identified as sulfite oxidase deficient and to an animal model of the disease are discussed.
Authors
J L Johnson, K V Rajagopalan
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