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[Cancer Research 25, 671-676, June 1, 1965]
© 1965 American Association for Cancer Research

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Patterns of Glycolytic Enzymes in Rat Liver and Hepatoma1

Carl E. Shonk, Harold P. Morris and George E. Boxer

( Merck, Sharp <-p; Dohme Research Laboratories, Division of Merck and Co., Inc., Rahway, New Jersey, and Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Public Health Service, Department of Health, Education and Welfare, Bethesda, Maryland)

Activities of glycolytic enzymes were determined under concordant conditions in a series of rat hepatomas and were compared to normal rat liver. The levels of the activities of certain enzymes were found to divide the hepatomas into 2 groups differing in growth rates. In the more rapidly growing hepatomas the activities of glucokinase, phosphofructokinase, and pyruvate kinase were elevated, whereas fructose diphosphatase, glycerolphosphate dehydrogenase, and phosphoglucomutase activities were drastically decreased. The malate dehydrogenases were also substantially reduced, but considerable enzymic activity still remained. These changes tend to diminish some of the specialized functions of normal liver and can be viewed as a graded dedifferentiation of the tissue.

1 This investigation was supported by the Cancer Chemotherapy National Service Center, National Cancer Institute, under the NIH contract No. SA-43-ph-1886.

Received 12/ 4/64.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1965 by the American Association for Cancer Research.