Ca2+-binding properties of a unique ATPase inhibitor protein isolated from mitochondria of bovine heart and rat skeletal muscle
- 31 December 1985
- journal article
- Published by Elsevier in Cell Calcium
- Vol. 6 (6), 469-479
- https://doi.org/10.1016/0143-4160(85)90022-3
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Isolation of two ATPase inhibitor proteins from mitochondria of rat skeletal muscleBioscience Reports, 1983
- Equilibrium binding of 125I-labeled adenosine triphosphatase inhibitor protein to complex V of the mitochondrial oxidative phosphorylation systemBiochemistry, 1982
- Spontaneous aggregation of the mitochondrial natural ATPase inhibitor in salt solutions as demonstrated by gel filtration and neutron scattering. Application to the concomitant purification of the ATPase inhibitor and F1-ATPaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
- Phenothiazines and related compounds disrupt mitochondrial energy production by a calmodulin-independent reactionBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
- Positive cooperative binding of calcium to bovine brain calmodulinBiochemistry, 1980
- [5] Preparation of bovine heart mitochondria in high yieldMethods in Enzymology, 1979
- Specificity of the binding of trifluoperazine to the calcium-dependent activator of phosphodiesterase and to a series of other calcium-binding proteinsBiochimica et Biophysica Acta (BBA) - General Subjects, 1978
- [14] Ligand-binding by associating systemsMethods in Enzymology, 1978
- [13] The meaning of scatchard and hill plotsMethods in Enzymology, 1978
- Cyclic 3′ : 5′-Nucleotide PhosphodiesterasePublished by Elsevier ,1974