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Presence and characterization of glycolipid sulfotransferase in human cancer serum.

Abstract
Sulfotransferase, which catalyzes sulfation of the carbohydrate of galactosylceramide (GalCer) and is localised in the Golgi membrane of cells, was assayed for activity in human serum. To do this, an organic solvent was added to the incubated reaction mixture containing GalCer as an acceptor and phosphoadenosine phospho[35S]-sulfate as a donor of sulfate to dissociate the synthesized sulfolipid from serum protein. This was followed by isolation of the sulfolipid on an anion-exchange column. Through this procedure, human serum was found to contain sulfotransferase activity. The serum enzyme was activated by Mn2+. Km values of the enzyme for GalCer and 'active sulfate' were 4.6 microM and 5.2 microM, respectively. The enzyme activity was assayed in sera of cancer patients. The serum activity (mean +/- SE, 0.27 +/- 0.027 pmol.microliter-1.h-1) in renal cell carcinoma patients, whose activity has been demonstrated to be elevated, was significantly (P less than 0.005) increased compared to that of the normal control (mean +/- SE, 0.18 +/- 0.0014 pmol.microliter-1.h-1) and of other urological tumors examined.
AuthorsS Gasa, M T Casl, A Makita, N Sakakibara, T Koyanagi, T Atsuta
JournalEuropean journal of biochemistry (Eur J Biochem) Vol. 189 Issue 2 Pg. 301-6 (Apr 30 1990) ISSN: 0014-2956 [Print] England
PMID2338078 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Biomarkers, Tumor
  • Cations, Divalent
  • Sulfurtransferases
  • Sulfotransferases
  • galactosylceramide sulfotransferase
Topics
  • Biomarkers, Tumor (blood)
  • Cations, Divalent (pharmacology)
  • Colonic Neoplasms (enzymology)
  • Humans
  • Kinetics
  • Lung Neoplasms (enzymology)
  • Male
  • Neoplasms (blood, enzymology)
  • Reference Values
  • Stomach Neoplasms (enzymology)
  • Substrate Specificity
  • Sulfotransferases
  • Sulfurtransferases (blood)
  • Testicular Neoplasms (enzymology)
  • Urinary Bladder Neoplasms (enzymology)

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