Characterization of the energy-dependent calcium binding of a mitochondrial fraction isolated from bovine intrapulmonary vein

1979 ◽  
Vol 57 (10) ◽  
pp. 1107-1113 ◽  
Author(s):  
Dennis B. McNamara ◽  
Marie-Jeanne Roulet ◽  
Albert L. Hyman ◽  
Philip J. Kadowitz

A mitochondrial-enriched fraction was isolated from bovine intrapulmonary vein; this fraction had a three- to four-fold enrichment factor for succinic dehydrogenase, a mitochondrial marker enzyme, and bound calcium in an azide-sensitive, energy-dependent fashion using either ATP or succinate as substrate. The calcium binding was sensitive to the concentrations of H+, ATP, Ca2+, and mitochondrial fraction. Binding and accumulation were time dependent, reaching at 10–12 min a plateau which was maintained over the time interval studied, i.e. 18 min. At the plateau, maximal binding was 221 ± 8.64 and maximal accumulation was 285 ± 20.2 nmol Ca2+/mg protein. The mitochondrial-enriched fraction contained an azide-sensitive, Mg2+-dependent, Ca2+-stimulated ATPase (Mg2+ + Ca2+ = 25.59 ± 1.03, Ca2+ = 3.96 ± 1.06 μmol P1/mg protein per hour). This study is the first to report the isolation from intrapulmonary vein of a subcellular organelle capable of binding calcium in an energy-dependent fashion; furthermore, it confirms and extends the observations of others that mitochondria may contribute to intracellular calcium homeostasis in vascular smooth muscle.

1975 ◽  
Vol 229 (3) ◽  
pp. 801-806 ◽  
Author(s):  
RJ Solomon ◽  
P Silva ◽  
Bend ◽  
FH Epstein

Adenosine triphosphatase activity not dependent on sodium or potassium but inhibited by thiocyanate is present in broken-cell homogenates of eel gill and rat kidney. This enzymatic property is predominantly associated with mitochondria, although thiocyanate-inhibited ATPase can also be detected in microsomes with little or no mitochondrial contamination as measured by the activity of the mitochondrial marker enzyme succinic dehydrogenase. When eels are transferred from fresh to salf water, thus increasing active outward transport of chloride across the gill, the thiocyanate-inhibited ATPase of gill microsomes does not change, though the activities of succinic dehydrogenase and Na-K-ATPase in gill homogenates are augmented. The thiocyanate-inhibited ATPase of homogenates of outer renal medulla does not differ from that of renal cortex, in contrast to Na-k-atpase which is higher in renal medulla than in cortex. The data do not support a role for thiocyanate-inhibited ATPase in active chloride transport by epithelial tissues.


1976 ◽  
Vol 251 (17) ◽  
pp. 5345-5351
Author(s):  
J M McDonald ◽  
D E Bruns ◽  
L Jarett

FEBS Letters ◽  
1995 ◽  
Vol 362 (1) ◽  
pp. 55-58 ◽  
Author(s):  
Lazaros T Kakalis ◽  
Michael Kennedy ◽  
Robert Sikkink ◽  
Frank Rusnak ◽  
Ian M Armitage

1993 ◽  
Vol 318 ◽  
Author(s):  
Q. Jiang ◽  
A. Chan ◽  
Y.-L. He ◽  
G.-C. Wang

ABSTRACTThe growth and chemical intermixing of submonolayer and a few monolayer thick Fe films on a Au(001) surface was studied by High Resolution Low Energy Electron Diffraction (HRLEED) technique. Through the analysis of the energy dependent angular profiles as a function of time, we obtained the distribution of islands and distribution of spacings during submonolayer growth. The interference of electron waves from different chemical elements in terraces at different heights in the surface contributes to the background intensity and broadening in the angular profiles of diffraction beams. A subsurface Fe capped by Au islands as a result of atomic place exchange was observed at the initial stage of monolayer growth. From the energy dependent angular profiles as a function of temperature, we determine the quantitative change of inhomogeneity length (∼20 Å) at the interface of ultrathin films at elevated temperatures due to intermixing.


FEBS Letters ◽  
1982 ◽  
Vol 142 (1) ◽  
pp. 115-117 ◽  
Author(s):  
V.I. Negruk ◽  
D.I. Cherny ◽  
I.D. Nikiforova ◽  
A.A. Aleksandrov ◽  
R.G. Butenko

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