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Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues.
J Clin Invest. 1987 Jun; 79(6):1564-70.JCI

Abstract

In response to global ischemia, tissue xanthine dehydrogenase was converted to xanthine oxidase in all tissues with half-times of conversion at 37 degrees C of approximately 3.6, 6, 7, and 14 h for the liver, kidney, heart, and lung, respectively. The time course of enzyme conversion at 4 degrees C was greatly extended with half-conversion times of 6, 5, 5, and 6 d for the respective tissues. Increases in xanthine oxidase activity were accompanied by the appearance of a distinct new protein species with greater electrophoretic mobility. The oxidase from ischemic rat liver was purified 781-fold and found to migrate with a higher mobility on native gels than the purified native dehydrogenase. Sodium dodecyl sulfate profiles revealed the presence of a single major band of 137 kD for the native dehydrogenase, whereas the oxidase had been partially cleaved generating polypeptides of 127, 91, and 57 kD. Polypeptide patterns for the oxidase resemble those seen following limited in vitro proteolysis of the native dehydrogenase supporting a proteolytic mechanism for the conversion of xanthine dehydrogenase to oxidase in ischemic rat liver.

Authors

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Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

3294898

Citation

Engerson, T D., et al. "Conversion of Xanthine Dehydrogenase to Oxidase in Ischemic Rat Tissues." The Journal of Clinical Investigation, vol. 79, no. 6, 1987, pp. 1564-70.
Engerson TD, McKelvey TG, Rhyne DB, et al. Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. J Clin Invest. 1987;79(6):1564-70.
Engerson, T. D., McKelvey, T. G., Rhyne, D. B., Boggio, E. B., Snyder, S. J., & Jones, H. P. (1987). Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. The Journal of Clinical Investigation, 79(6), 1564-70.
Engerson TD, et al. Conversion of Xanthine Dehydrogenase to Oxidase in Ischemic Rat Tissues. J Clin Invest. 1987;79(6):1564-70. PubMed PMID: 3294898.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. AU - Engerson,T D, AU - McKelvey,T G, AU - Rhyne,D B, AU - Boggio,E B, AU - Snyder,S J, AU - Jones,H P, PY - 1987/6/1/pubmed PY - 1987/6/1/medline PY - 1987/6/1/entrez SP - 1564 EP - 70 JF - The Journal of clinical investigation JO - J Clin Invest VL - 79 IS - 6 N2 - In response to global ischemia, tissue xanthine dehydrogenase was converted to xanthine oxidase in all tissues with half-times of conversion at 37 degrees C of approximately 3.6, 6, 7, and 14 h for the liver, kidney, heart, and lung, respectively. The time course of enzyme conversion at 4 degrees C was greatly extended with half-conversion times of 6, 5, 5, and 6 d for the respective tissues. Increases in xanthine oxidase activity were accompanied by the appearance of a distinct new protein species with greater electrophoretic mobility. The oxidase from ischemic rat liver was purified 781-fold and found to migrate with a higher mobility on native gels than the purified native dehydrogenase. Sodium dodecyl sulfate profiles revealed the presence of a single major band of 137 kD for the native dehydrogenase, whereas the oxidase had been partially cleaved generating polypeptides of 127, 91, and 57 kD. Polypeptide patterns for the oxidase resemble those seen following limited in vitro proteolysis of the native dehydrogenase supporting a proteolytic mechanism for the conversion of xanthine dehydrogenase to oxidase in ischemic rat liver. SN - 0021-9738 UR - https://www.unboundmedicine.com/medline/citation/3294898/Conversion_of_xanthine_dehydrogenase_to_oxidase_in_ischemic_rat_tissues_ L2 - https://doi.org/10.1172/JCI112990 DB - PRIME DP - Unbound Medicine ER -