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Human colon tumors: enzymic and histological characteristics.

Abstract
In samples of colonic adenocarcinomas, the mean activities of thymidine kinase, glucose-6-phosphate dehydrogenase, phosphoserine phosphatase and pyrroline-5-carboxylate reductase were several fold higher than those of nonneoplastic colon. The presence of considerable, cold labile pyrroline-5-carboxylate reductase activity provided an additional criterion for distinguishing tumors from the control tissue. Deviations from the pattern of enzymes in normal colon were much more pronounced in the five moderately well-differentiated than in the single well-differentiated adenocarcinoma.
AuthorsA Herzfeld, M A Legg, O Greengard
JournalCancer (Cancer) Vol. 42 Issue 3 Pg. 1280-3 (Sep 1978) ISSN: 0008-543X [Print] UNITED STATES
PMID212173 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Organophosphorus Compounds
  • Serine
  • Glucosephosphate Dehydrogenase
  • Pyrroline Carboxylate Reductases
  • Thymidine Kinase
  • Phosphoric Monoester Hydrolases
Topics
  • Adenocarcinoma (enzymology, pathology)
  • Cell Differentiation
  • Colonic Neoplasms (enzymology, pathology)
  • Glucosephosphate Dehydrogenase (metabolism)
  • Humans
  • Organophosphorus Compounds
  • Phosphoric Monoester Hydrolases (metabolism)
  • Pyrroline Carboxylate Reductases (metabolism)
  • Serine
  • Thymidine Kinase (metabolism)

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