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Gene Review

SORD  -  sorbitol dehydrogenase

Bos taurus

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Disease relevance of SORD


High impact information on SORD

  • The effect of ATP in enhancing alpha-crystallin-promoted SDH renaturation appears to be both nonspecific and to not involve hydrolysis phenomena, thus confirming that the chaperone action of alpha-crystallin is not dependent on ATP as energy donor [4].
  • Here we report that alpha-crystallin, in the presence of the SDH pyridine cofactor NAD(H), can exert a remarkable chaperone action by favoring the recovery of the enzyme activity from chemically denaturated SDH up to 77% [4].
  • Sorbitol dehydrogenase (EC was isolated from bovine brain and purified 3,000-fold to apparent homogeneity, as judged by polyacrylamide gel electrophoresis [5].
  • The enzyme is also inactivated by thiol-blocking reagents; with respect to inactivation by sodium pyrophosphate, sorbitol dehydrogenase is different from closely related alcohol dehydrogenase [5].
  • The method is based on reduction of fructose by a commercially available preparation of sorbitol dehydrogenase (EC, with the concomitant oxidation of NADH [6].

Biological context of SORD

  • These data were compared to independently and concurrently obtained measurements of emboli shear rate (CPF), platelet count, red blood count (RBC), leukocyte count (WBC), plasma free hemoglobin, factors XIII, X, and V, and sorbitol dehydrogenase [7].

Anatomical context of SORD


Associations of SORD with chemical compounds


Other interactions of SORD


  1. Use of physiologic variables to predict milk yield after clinical mastitis in dairy cattle. Sischo, W.M., Moore, D.A., Fedon, J.C. J. Am. Vet. Med. Assoc. (1997) [Pubmed]
  2. Hyperlipemia and ketonuria in an alpaca and a llama. Anderson, D.E., Constable, P.D., Yvorchuk, K.E., Anderson, N.V., St-Jean, G., Rock, L. J. Vet. Intern. Med. (1994) [Pubmed]
  3. Serological and biochemical follow-up in cattle naturally infected with Fasciola hepatica, and comparison with a climate model for predicting risks of fasciolosis. Bossaert, K., Lonneux, J.F., Godeau, J.M., Peeters, J., Losson, B. Vet. Res. (1999) [Pubmed]
  4. Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase. Marini, I., Moschini, R., Del Corso, A., Mura, U. Cell. Mol. Life Sci. (2005) [Pubmed]
  5. Purification and characterization of sorbitol dehydrogenase from bovine brain. Wiesinger, H., Hamprecht, B. J. Neurochem. (1989) [Pubmed]
  6. Enzymic determination of fructose in seminal plasma by initial rate analysis. Anderson, R.A., Reddy, J.M., Oswald, C., Zaneveld, L.J. Clin. Chem. (1979) [Pubmed]
  7. Light scattering detection of microemboli in an extracorporeal LVAD bovine model. Reynolds, L.O., Mohammad, S.F., Solen, K.A., Pantalos, G.M., Burns, G.L., Olsen, D.B. ASAIO transactions / American Society for Artificial Internal Organs. (1990) [Pubmed]
  8. Milk transfer of pyrrolizidine alkoloids in cattle. Dickinson, J.O., Cooke, M.P., King, R.R., Mohamed, P.A. J. Am. Vet. Med. Assoc. (1976) [Pubmed]
  9. The effect of protein intake on the activities of liver specific enzymes in the plasma of dairy cows. Treacher, R.J., Collis, K.A. Res. Vet. Sci. (1977) [Pubmed]
  10. The excretion of phylloerythrin and bilirubin by calves and sheep. Ford, E.J., Gopinath, C. Res. Vet. Sci. (1976) [Pubmed]
  11. Serum biochemical and hematologic values of normal and Mycobacterium bovis-infected American bison. Miller, L.D., Thoen, C.O., Throlson, K.J., Himes, E.M., Morgan, R.L. J. Vet. Diagn. Invest. (1989) [Pubmed]
  12. Kochia scoparia poisoning in cattle. Dickie, C.W., James, L.F. J. Am. Vet. Med. Assoc. (1983) [Pubmed]
  13. Biochemical indicators of liver injury in calves with experimental fascioliasis. Anderson, P.H., Berrett, S., Brush, P.J., Hebert, C.N., Parfitt, J.W., Patterson, D.S. Vet. Rec. (1977) [Pubmed]
  14. A simplified method for measuring activity of beta-D-fructofuranoside fructohydrolase (invertase). Boguslawski, G. J. Appl. Biochem. (1983) [Pubmed]
  15. NADPH-dependent reduction of glyceraldehyde: a unusually high activity in the lens of the camel (Camelus dromedarius). Del Corso, A., Osman, A.M., Mohamed, A.S., Camici, M., Barsacchi, D., Tozzi, M.G., Mura, U. Boll. Soc. Ital. Biol. Sper. (1989) [Pubmed]
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