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J. Biol. Chem., Vol. 261, Issue 6, 2567-2574, Feb, 1986
BE Corkey, J Duszynski, TL Rich, B Matschinsky and JR Williamson
Null point titration techniques have been developed for measurements of
cytosolic free Mg2+ in isolated cells and matrix free Mg2+ in isolated
mitochondria using antipyrylazo III as a spectrophotometric Mg2+ indicator.
A cytosolic free Mg2+ of 0.37 +/- 0.02 mM was obtained with hepatocytes.
This represented about 6% of the total cytosolic magnesium content
(activity coefficient of 5.8 X 10(-2). Nondiffusable Mg2+- binding sites in
the cytosol were equal to 11.1 nmol/mg cell dry weight with an apparent
dissociation constant of 0.71 mM and accounted for binding of 32% of the
cytosolic magnesium. The null point method gave a value of 0.35 +/- 0.01 mM
for the mitochondrial matrix free Mg2+ concentration (activity coefficient
of 8.8 X 10(-3). Nondiffusable Mg2+ binding sites in the mitochondria were
estimated at 25.7 nmol/mg mitochondrial protein with an apparent
dissociation constant of 0.22 mM, compared with an apparent dissociation
constant of 1.66 microM for bound calcium. These data demonstrate the
absence of a significant gradient of free Mg2+ between the cytosolic and
mitochondrial compartments. They also demonstrate a high ligand binding
capacity for magnesium in both compartments with relatively low affinity
resulting in a constant value for free Mg2+ when total cell magnesium is
constant. This maintains a ratio between free Mg2+ and free Ca2+ of about
2000 in the cytosol and 100 in the mitochondria. The high concentration and
low affinity of Mg2+ binding sites results in rather large changes of free
Mg2+ with small variations in total cell magnesium. This is apparent in
hepatocytes isolated from streptozotocin diabetic rats which had a
decreased total magnesium content and a cytosolic free Mg2+ of 0.16 +/-
0.02 mM.
Regulation of free and bound magnesium in rat hepatocytes and isolated mitochondria
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