|
|
||||||||
Biology of Reproduction, Vol 12, 408-414, Copyright © 1975 by Society for the Study of Reproduction
1 Division of Perinatal Biology. Oregon Regional Primate Research Center, Beaverton, Oregon 97005, and
Department of Biochemistry, University of Oregon Medical School, Portland, Oregon 97201 Biopsies of myometrium from pregnant rhesus monkeys and taenia coli from nonpregnant monkeys
were rapidly excised and freeze-clamped. Tissue levels of all the metabolic intermediates and cofactors
of the glycolytic pathway were determined and the mass-action ratios for each reaction calculated. The
apparent equilibrium constants were over 1000 times larger than the mass-action ratios for hexokinase,
phosphofructokinase, and pyruvic kinase; this is evidence that these three enzymes are rate-limiting for
glycolysis in both types of smooth muscle. The apparent equilibrium constants of the combined reaction
for glyceraldehyde-P dehydrogenase plus P-glycerate kinase were 30 and 50 times greater than the
mass-action ratios for myometrium and taenia coli respectively: thus it is possible that this step is also
rate-limiting. The remaining reactions in glycolysis are either at equilibrium or fairly close to
equilibrium and therefore cannot be rate-limiting. The conversion of [14C] fructose-6-P to [14C] lactate by cell-free extracts of myometrium and taenia
coli was studied. Without added ATP, no [14C] lactate was produced, increasing the level of ATP
increased and then decreased lactate production. This biphasic response to increasing levels of ATP is
also found in semipurified preparations of cardiac and skeletal muscle phosphofructokinase. As in
cardiac and skeletal muscle, the ATP inhibition of [14C] lactate production by myometrium was relieved
by inorganic phosphate.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |