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Fructose 2,6‐bisphosphate in isolated foetal hepatocytes
Author(s) -
Martín-Sanz Paloma,
Cascales María,
Boscá Lisardo
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81127-4
Subject(s) - fructose 2,6 bisphosphate , pyruvate kinase , glycerol kinase , glucagon , incubation , phosphofructokinase 2 , enzyme , biochemistry , fructose , chemistry , kinase , protein subunit , biology , microbiology and biotechnology , glycolysis , hormone , phosphofructokinase , gene
Fru 2,6‐P 2 was present in isolated foetal hepatocytes at a concentration of 1.6 nmol per g cells. When foetal hepatocytes were exposed to glucagon no changes were observed either in the concentration of Fru 2,6‐P 2 and lactate release or in the activities of 6‐phosphofructo‐2‐kinase and pyruvate kinase. Incubation of purified 6‐phosphofructo‐2‐kinase with the catalytic subunit of protein kinase did not change the enzyme activity. The inhibition by sn ‐glycerol 3‐phosphate was much lower for the foetal than for adult enzyme. These results suggest that an isoenzyme of 6‐phosphofructo‐2‐kinase in foetal hepatocytes different from that of adult hepatocytes may be present.