Open AccessHeterogeneous Distribution of ATP Citrate Lyase in Rat‐Liver Parenchyma
Author(s) -
KATZ Norbert R.,
FISCHER Wilhelm,
ICK Margit
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07151.x
Subject(s) - atp citrate lyase , lyase , parenchyma , glycolysis , enzyme , biochemistry , coenzyme a , metabolism , endocrinology , medicine , biology , chemistry , citrate synthase , reductase , botany
1 A radiochemical microtest was established for the determination of ATP citrate lyase in tissue samples of 0.2–1.0 μg dry weight. The specificity of this test system was guaranteed by its coenzyme A dependence as well as by inhibition of the activity measured in presence of a specific antibody. 2 Using this test system ATP citrate lyase activity was determined in microdissected periportal and perivenous liver tissue of fed, fasted and refed animals. The perivenous activity was 1.8‐fold and 2.4‐fold higher than the periportal one in fed male and female rats respectively. 3 The perivenous to periportal gradient was decreased during starvation‐dependent reduction of the ATP citrate lyase activity. On the other hand it was not only restored but enhanced up to 2.8 after refeeding‐dependent enhancement of the enzyme activity. 4 The predominance of the ATP citrate lyase activity in the perivenous, mainly glycolytic zone supports the hypothesis of the coordinate zonation of the carbohydrate and the lipid metabolism in the liver parenchyma.