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1.
Summary Two-dimensional crystalline arrays of Ca2+-ATPase molecules develop after treatment of sarcoplasmic reticulum vesicles with Na3VO4 in a Ca2+-free medium. The influence of membrane potential upon the rate of crystallization was studied by ion substitution using oxonol VI and 3,3-diethyl-2,2-thiadicarbocyanine (Di–S–C2(5)) to monitor inside positive or inside negative membrane, potentials, respectively. Positive transmembrane potential accelerates the rate of crystallization of Ca2+-ATPase, while negative potential disrupts preformed Ca2+-ATPase crystals, suggesting an influence of transmembrane potential upon the conformation of Ca2+-ATPase. 相似文献
2.
R 24571: a new powerful inhibitor of red blood cell Ca++-transport ATPase and of calmodulin-regulated functions 总被引:21,自引:0,他引:21
K Gietzen A Wüthrich H Bader 《Biochemical and biophysical research communications》1981,101(2):418-425
Compound R 24571 (1-[bis(p-chlorophenyl)methyl]-3-[2,4-dichloro-β-(2,4-dichlorobenzyloxy)phenethyl]imidazoliniumchloride) is found to be a powerful inhibitor of red blood cell Ca++-ATPase as well as Ca++ transport into inside-out red blood cell vesicles with an IC50-value of 0.5 and 2 μM, respectively. The inhibitory action of R 24571 is more specific on the calmodulin-dependent fraction of Ca++-transport ATPase as compared to the basal Ca++-transport ATPase (determined in the absence of calmodulin) and can be antagonized by increasing concentrations of calmodulin in an apparently competitive manner. With respect to other ATPases the action of R 24571 is relatively specific for red blood cell Ca++-transport ATPase. Mg++-ATPase requires a 40 times higher concentration for halfmaximal inhibition (IC50 = 20 μM) whereas (Na+ + K+)-transport ATPase is only slightly affected in the investigated concentration range (≤20 μM). 相似文献
3.
4.
Takashi Daiho Kazuo Yamasaki Stefania Danko Hiroshi Suzuki 《The Journal of biological chemistry》2014,289(45):31241-31252
The actuator (A) domain of sarco(endo)plasmic reticulum Ca2+-ATPase not only plays a catalytic role but also undergoes large rotational movements that influence the distant transport sites through connections with transmembrane helices M1 and M2. Here we explore the importance of long helix M2 and its junction with the A domain by disrupting the helix structure and elongating with insertions of five glycine residues. Insertions into the membrane region of M2 and the top junctional segment impair Ca2+ transport despite reasonable ATPase activity, indicating that they are uncoupled. These mutants fail to occlude Ca2+. Those at the top segment also exhibited accelerated phosphoenzyme isomerization E1P → E2P. Insertions into the middle of M2 markedly accelerate E2P hydrolysis and cause strong resistance to inhibition by luminal Ca2+. Insertions along almost the entire M2 region inhibit the dephosphorylated enzyme transition E2 → E1. The results pinpoint which parts of M2 control cytoplasm gating and which are critical for luminal gating at each stage in the transport cycle and suggest that proper gate function requires appropriate interactions, tension, and/or rigidity in the M2 region at appropriate times for coupling with A domain movements and catalysis. 相似文献
5.
We propose an overview of the mechanism of Ca2+ transport through the sarcoplasmic reticulum membrane via the Ca2+-ATPase. We describe cytoplasmic calcium binding, calcium occlusion in the membrane and lumenal calcium dissociation. A channel-like structure is discussed and related to structural data on the membranous domain of the Ca2+-ATPase.Abbreviations SR
Sarcoplasmic Reticulum
- AMPPNP
adenylyl-imidodiphosphate
- AMPPCP
adenylyl (,-methylene)-diphosphonate
- FITC
fluorescein 5-isothiocyanate
- NBD
4-nitrobenzo-2-oxa-1,3-diazole
- DCCD
dicyclohexylcarbodiimide 相似文献
6.
The regulatory role of Ca2+-stimulated adenosine 5-triphosphatase (Ca2+-ATPase) in Ca2+ transport system of rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+-ATPase activity was calculated by subtracting Mg2+-ATPase activity from (Ca2+–Mg2+)-ATPase activity. The release of Ca2+ from the Ca2+-loaded nuclei was evoked progressively after Ca2+ uptake with 1.0 mM ATP addition, while it was only slightly in the case of 2.0 mM ATP addition, indicating that the consumption of ATP causes a leak of Ca2+ from the Ca2+-loaded nuclei. The presence of N-ethylmaleimide (NEM; 0.1 mM) caused an inhibition of nuclear Ca2+ uptake and induced a promotion of Ca2+ release from the Ca2+-loaded nuclei. NEM (0.1 and 0.2 mM) markedly inhibited nuclear Ca2+-ATPase activity. This inhibition was completely blocked by the presence of dithiothreitol (DTT; 0.1 and 0.5 mM). Also, DTT inhibited the effect of NEM (0.1 mM) on nuclear Ca2+ uptake and release. Meanwhile, verapamil and diltiazem (10 M), a blocker of Ca2+ channels, did not prevent the NAD+ (1.0 and 2.0 mM), zinc sulfate (1.0 and 2.5 M) and arachidonic acid (10 M)-induced increase in nuclear Ca2+ release, suggesting that Ca2+ channels do not involve on Ca2+ release from the nuclei. These results indicates that an inhibition of nuclear Ca2+-ATPase activity causes the decrease in nuclear Ca2+ uptake and the release of Ca2+ from the Ca2+-loaded nuclei. The present finding suggests that Ca2+-ATPase plays a critical role in the regulatory mechanism of Ca2+ uptake and release in rat liver nuclei. 相似文献
7.
The kinetic properties of active Ca2+ transport into mitochondria and microsomal membrane vesicles prepared from coleoptiles of dark-and light-grown corn seedlings have been studied. The apparent values for K m and V max for Ca2+ of the mitochondrial transport system from dark-grown plants are about one order of magnitude higher than those from the microsomal transport system. Calmodulin has no effect on the Ca2+ accumulation into mitochondria whereas the apparent maximum transport velocity and affinity for Ca2+ of the microsomal Ca2+-transport system are both increased by calmodulin. When intact corn seedlings are irradiated with far-red light, the calmodulin-induced increase of the apparent maximum transport velocity and affinity for Ca2+ can no longer be observed. From these data it can be concluded that the low cytoplasmic Ca2+ concentration in the cytoplasm of coleoptile cells from dark-grown corn is maintained by a calmodulin-regulated Ca2+ pump. Irradiation with photomorphogenically active far-red light lowers the Ca2+-transport activity and thus causes an increase of the cytoplasmic, free-Ca2+ concentration. The physiological implications will be discussed. 相似文献
8.
Chengjing Cao Timothy Lockwich Terrence L. Scott Robert Blumenthal Adil E. Shamoo 《Molecular and cellular biochemistry》1991,103(2):97-111
Summary In reconstituted rabbit skeletal muscle (Ca2+ + Mg2+)-ATPase proteoliposomes, Ca2+-uptake is decreased by more than 90% with T2 cleavage (Arg-198). However, no difference in the ATP dependence of hydrolysis activity is seen between SR and trypsin-treated SR. A large decrease in E-P formation and hydrolysis activity of the enzyme appear only at T3 cleavage, which represents the cleavage of A1 fragment to A1a + A1b forms. The disappearance of hydrolysis activity due to digestion is prior to the disappearance of E-P formation. No significant difference is found in the passive Ca2+ efflux between control SR and tryptically digested SR in the absence of Mg+ ruthenium red or in the presence of ATP. However, the passive Ca2+ efflux rate for tryptically digested SR is much larger than control SR in the presence of Mg2+ + ruthenium red. These results show that the Ca2+ channel cannot be closed after trypsin digestion of SR membranes by the presence of the Ca2+ channel inhibitors, Mg2+ and ruthenium red. In the reconstituted ATPase proteoliposomes, the Ca2+ efflux rates are the same regardless of digestion (T2); also, efflux is not affected by the presence or absence of Mg2+ + ruthenium red. These results indicate that T2 cleavage causes uncoupling of the Ca2+-pump from ATP hydrolytic activity.A theoretical model is developed in order to fit the extent of tryptic digestion of the A fragment of the (Ca2+ + Mg2+)-ATPase polypeptide with the loss of Ca2+-transport. Fits of the theoretical equations to the data are consistent with that Ca2+-transport system appears to require a dimer of the polypeptide (Ca2+ + Mg2+)-ATPase. 相似文献
9.
Toyoshima C 《Archives of biochemistry and biophysics》2008,476(1):3-11
Ca2+-ATPase of muscle sarcoplasmic reticulum is an ATP-powered Ca2+-pump that establishes a >10,000-fold concentration gradient across the membrane. Its crystal structures have been determined for nine different states that cover nearly the entire reaction cycle. Presented here is a brief structural account of the ion pumping process, which is achieved by a series of very large domain rearrangements. 相似文献
10.
Rajesh Mahey Michael A. Bridges Sidney Katz 《Molecular and cellular biochemistry》1991,105(2):137-147
Partially purified plasma membrane fractions were prepared from guinea-pig pancreatic acini. These membrane preparations were found to contain an ATP-dependent Ca2+-transporter as well as a heterogenous ATP-hydrolytic activity. The Ca2+-transporter showed high affinity for Ca2+ (KCa
2+ = 0.04 ± 0.01 M), an apparent requirement for Mg2+ and high substrate specificity. The major component of ATPase activity could be stimulated by either Ca2+ or Mg2+ but showed a low affinity for these cations. At low concentrations, Mg2+ appeared to inhibit the Ca2+-dependent ATPase activity expressed by these membranes. However, in the presence of high Mg2+ concentration (0.5–1 mM), a high affinity Ca2+-dependent ATPase activity was observed (KCa
2+ = 0.08 ± 0.02 M). The hydrolytic activity showed little specificity towards ATP. Neither the Ca2+-transport nor high affinity Ca2+-ATPase activity were stimulated by calmodulin. The results demonstrate, in addition to a low affinity Ca2+ (or Mg+)-ATPase activity, the presence of both a high affinity Ca2+-pump and high affinity Ca2+-dependent ATPase. However, the high affinity Ca2+-ATPase activity does not appear to be the biochemical expression of the Ca2+-pump.Abbreviations Ca2+-ATPase
calcium-activated, magnesium-dependent adenosine triphosphatase
- CaM
calmodulin
- CDTA
trans-1,2-diaminocyclohexane-N,N,N,N-tetraacetate
- EDTA
ethylene-diaminetetraacetate
- EGTA
ethylene glycol bis(-aminoethyl ether)-N,N,N,N-tetraacetate
- NADPH
reduced form of nicotinamide adenine dinucleotide phosphate 相似文献
11.
A mitochondria-free membrane fraction prepared from rat myometrium accumulated 45Ca2+ in the presence of oxalic acid and ATP. The rate of transport of Ca2+ into the membranous vesicles was increased by greater than 50% in the presence of 3′,5′-cyclic AMP, but not by 2′,3′-cyclic AMP or 5′-AMP. Membrane ATPase activity was stimulated by cyclic AMP in a manner similar to Ca2+-transport. ATPase activity was stimulated by Mg2+; slight additional stimulation was obtained in the presence of Na+ and K+ but not in the presence of Ca2+. Despite the cyclic AMP sensitivity of membrane ATPase activity, the absence of any effect of inhibitors of Ca2+-transport suggest it has little to do with Ca2+ accumulation by the membranes.Cyclic AMP-induced increase in Ca2+-transport and membrane ATPase activity was duplicated in vivo by incubating uteri in 10−4 M isoproterenol prior to membrane isolation. Isoproterenol has been previously shown to increase myometrial cyclic AMP levels, and changes in Ca2+-transport by cell membranes in relation to intracellular cyclic AMP levels may be the mechanism through which hormones modulate uterine contractility. 相似文献
12.
《The International journal of biochemistry》1980,11(4):583-589
- 1.1. Activation of Mg2+-ATPase of rabbit and guinea-pig erythrocyte membrane by bicarbonate or chloride could be completely abolished by ethylene-glycol-bis-(β-aminoethylether)-N,N'-tetraacetic acid. The anion stimulation was actually an activation of contaminating Ca2+ -stimulated Mg2+-ATPase by monovalent cations associated with the anions.
- 2.2. Guinea-pig red cell Ca2+-Mg2+-ATPase could be activated by both sodium and potassium while the rabbit enzyme was sensitive only to sodium. The concentrations of monovalent cations for half-maximal stimulation of Ca2+-Mg2+-ATPase are: kna+ = 40.8 mM, kk+ = 12.2 mM (guinea-pig); KNa+ = 13.3mM (rabbit).
- 3.3. Potassium enhanced activation of rabbit erythrocyte membrane Ca2+-Mg2+-ATPase by red cell Ca2+-Mg2+-ATPase activator protein. With the guinea pig enzyme, neither sodium nor potassium enhanced activator stimulation of Ca2+-Mg2+-ATPase.
- 4.4. Ca2+-Mg2+-ATPase of aged rabbit erythrocyte membrane responded to sodium but not to activator protein.
- 5.5. Triton X-100 solubilized rabbit erythrocyte membrane Ca2+-Mg2+-ATPase has an apparent molecular weight of 371,000. It did not respond to the activator.
- 6.6. One major and three minor proteins, visualized by SDS-polyacrylamide gel electrophoresis, were extracted from rabbit erythrocyte membrane by 50 μM chlorpromazine.
13.
The role of Ca2+-stimulated adenosine 5-triphosphatase (Ca2+-ATPase) in Ca2+ sequestering of rat liver nuclei was investigated. Ca2+-ATPase activity was calculated by subtracting Mg2+-ATPase activity from (Ca2+–Mg2+)-ATPase activity. Ca2+ uptake and release were determined with a Ca2+ electrode. Nuclear Ca2+-ATPase activity increased linearly in the range of 10–40 M Ca2+ addition. With those concentrations, Ca2+ was completely taken up by the nuclei dependently on ATP (2 mM). Nuclear Ca2+-ATPase activity was decreased significantly by the presence of arachidonic acid (25 and 50 M), nicotinamide-adenine dinucleotide (NAD+; 2 mM) and zinc sulfate (2.5 and 5.0 M). These reagents caused a significant decrease in the nuclear Ca2+ uptake and a corresponding elevation in Ca2+ release from the nuclei. Moreover, calmodulin (10 g/ml) increased significantly nuclear Ca2+-ATPase activity, and this increase was not seen in the presence of trifluoperazine (10 M), an antogonist of calmodulin. The present findings suggest that Ca2+-ATPase plays a role in Ca2+ sequestering by rat liver nuclei, and that calmodulin is an activator. Moreover, the inhibition of Ca2+-ATPase may evoke Ca2+ release from the Ca2+-loaded nuclei. 相似文献
14.
《Comparative biochemistry and physiology. B, Comparative biochemistry》1993,104(3):719-728
- 1.1. Two components of Ca2+-Mg2+-ATPase are observed in kidneys of G. mirabilis. The high-affinity component has a K0.5Ca of 0.23μM; the low-affinity activity K0.5Ca is 90–110μM. The high-affinity activity requires Mg2+, displays Michaelis-Menten kinetics, has peak activity at 1.2 μM Ca2+, and is insensitive to ouabain and Na+ azide.
- 2.2. In subcellular fractions, the high-affinity component segregates with Na+-K+-ATPase and is localized predominantly in BLM. The low-affinity component is broadly distributed among membranous organelles, including brush border, and may be equivalent to alkaline phosphatase.
- 3.3. Specific activity of the high-affinity Ca2+-Mg2+-ATPase is modestly increased following adaptation of fish to FW, but total renal high-affinity activity is greatest in the hypertrophied kidneys of FW-adapted fish and is least in kidneys of fish adapted to 200% SW.
- 4.4. High-affinity Ca2+-Mg2+-ATPase may be associated with active Ca2+ transport or with regulation of intracellular Ca2+ concentration of tubular cells.
15.
16.
Effects of endotoxin administration on the ATP-dependent Ca2+ transport in canine cardiac sarcolemma were investigated. The results show that the sidedness of the sarcolemmal vesicles was not affected but the ATP-dependent Ca2+ transport in cardiac sarcolemma was decreased by 22 to 46% (p < 0.05) at 4 h following endotoxin administration. The kinetic analysis indicates that the Vmax for ATP and for Ca2+ were decreased by 50% (p < 0.01) and 32% (p < 0.01), respectively, while the Km values for ATP and Ca2+ were not significantly affected after endotoxin administration. Magnesium (1–5 mM) stimulated while vanadate (0.25–3.0 M) inhibited the ATP-dependent Ca2+ transport, but the Mg2+-stimulated and the vanadate-inhibitable activities remained significantly lower in the endotoxin-treated animals. These data demonstrate that endotoxin administration impairs the ATP-dependent Ca2+ transport in canine cardiac sarcolemma and that the impairment is associated with a mechanism not affecting the affinity towards ATP and Ca2+. Additional experiments show that the Ca2+ sensitivity of the Ca2+-ATPase activity was indifferent between the control and endotoxic groups suggesting that endotoxic injury impairs Ca2+ pumping without affecting Ca2+-ATPase activity. Since sarcolemmal ATP-dependent Ca2+ transport plays an important role in the regulation of cytosolic Ca2+ homeostasis, an impairment in the sarcolemmal ATP-dependent Ca2+ transport induced by endotoxin administration may have a pathophysiological significance in contributing to the development of myocardial dysfunction in endotoxin shock. 相似文献
17.
Summary Activities of Ca2+-dependent ATPase, Mg2+-dependent ATPase, Na+-K+-dependent ATP-ase, alkaline phosphatase, and 5-nucleotidase were demonstrated after incubation of 40-m vibratome sections of bovine parathyroids and subsequent visualization by electron microscopy. Prior to sectioning, parathyroid tissue was fixed with 1% glutaraldehyde for localization of alkaline phosphatase, and with 2% formaldehyde and 1% glutaraldehyde for demonstration activities of ATPases and 5-nucleotidase. The activities of the five enzymes were found at the apicolateral domain of the plasma membrane in parathyroid cells, i.e. at the site parathyroid cells face neighbouring parenchymal cells. Ca2+-ATPase activity was also seen on mitochondria, Golgi complex and RER. The presence of these plasma membrane associated enzymes at the apicolateral domain only indicate polarity in parathyroid cells. It further suggests that many processes including transmembrane transport take place at the apicolateral domain, the site of parathyroid cells opposing blood capillaries. 相似文献
18.
Kinetic properties of the ATP-dependent Ca2+ pump and the Na+/Ca2+ exchange system in basolateral membranes from rat kidney cortex 总被引:1,自引:0,他引:1
M. P. E. van Heeswijk J. A. M. Geertsen C. H. van Os 《The Journal of membrane biology》1984,79(1):19-31
Summary Basolateral plasma membranes from rat kidney cortex have been purified 40-fold by a combination of differential centrifugation, centrifugation in a discontinuous sucrose gradient followed by centrifugation in 8% percoll. The ratio of leaky membrane vesicles (L) versus right-side-out (RO) and inside-out (IO) resealed vesicles appeared to be LROIO=431. High-affinity Ca2+-ATPase, ATP-dependent Ca2+ transport and Na+/Ca2+ exchange have been studied with special emphasis on the relative transport capacities of the two Ca2+ transport systems. The kinetic parameters of Ca2+-ATPase activity in digitonin-treated membranes are:K
m
=0.11 m Ca2+ andV
max=81±4 nmol Pi/min·mg protein at 37°C. ATP-dependent Ca2+ transport amounts to 4.3±0.2 and 7.4±0.3 nmol Ca2+/min·mg protein at 25 and 37°C, respectively, with an affinity for Ca2+ of 0.13 and 0.07 m at 25 and 37°C. After correction for the percentage of IO-resealed vesicles involved in ATP-dependent Ca2+ transport, a stoichiometry of 0.7 mol Ca2+ transported per mol ATP is found for the Ca2+-ATPase. In the presence of 75mm Na+ in the incubation medium ATP-dependent Ca2+ uptake is inhibited 22%. When Na+ is present at 5mm an extra Ca2+ accumulation is observed which amounts to 15% of the ATP-dependent Ca2+ transport rate. This extra Ca2+ accumulation induced by low Na+ is fully inhibited by preincubation of the vesicles with 1mm ouabain, which indicates that (Na+–K+)-ATPase generates a Na+ gradient favorable for Ca2+ accumulation via the Na+/Ca2+ exchanger. In the absence of ATP, a Na+ gradient-dependent Ca2+ uptake is measured which rate amounts to 5% of the ATP-dependent Ca2+ transport capacity. The Na+ gradient-dependent Ca2+ uptake is abolished by the ionophore monensin but not influenced by the presence of valinomycin. The affinity of the Na+/Ca2+ exchange system for Ca2+ is between 0.1 and 0.2 m Ca2+, in the presence as well as in the absence of ATP. This affinity is surprisingly close to the affinity measured for the ATP-dependent Ca2+ pump. Based on these observations it is concluded that in isolated basolateral membranes from rat kidney cortex the Ca2+-ATPase system exceeds the capacity of the Na+/Ca2+ exchanger four- to fivefold and it is therefore unlikely that the latter system plays a primary role in the Ca2+ homeostasis of rat kidney cortex cells. 相似文献
19.
Sujata Persad Alena Vrbanova Johanna T. A. Meij Vincenzo Panagia Naranjan S. Dhalla 《Molecular and cellular biochemistry》1993,121(2):181-190
In order to investigate the involvement of phosphoinositide-specific phospholipase C (PLC), an enzyme associated with phosphoinositide signal transduction pathway, for the occurrence of Ca2+-paradox (loss of contractile activity associated with contracture), rat hearts perfused with Ca2+-free medium (1 to 5 min) were reperfused (5 to 10 min) with medium containing 1.25 mM Ca2+. Crude membranes isolated from hearts perfused with Ca2+-free medium exhibited a significantly increased activity of PLC, whereas normal activity was detected in hearts reperfused with Ca2+-containing medium. A significant rise in PLC activity was observed at 1 min of Ca2+-free perfusion; maximal increase was seen at 4 min of Ca2+-free perfusion. Minimal concentration of Ca2+ in the perfusion medium required for showing an increase in PLC activity was 10 M, whereas that required for the occurrence of Ca2+-paradoxic changes in heart function upon reperfusion was 50M. Perfusion of the hearts with Ca2+-free medium in the presence of low Na+ or at low temperature, which prevents the occurrence of Ca2+-paradox upon reperfusion, did not prevent the increase in PLC activity. An increase during Ca2+-free perfusion similar to that seen for PLC was also observed for two other enzymes, namely the phosphatidylinositol (PI) 4-kinase and the PI-4-monophosphate (PIP) 5-kinase, which synthesize the PLC substrate, phosphatidylinositol 4,5-bisphosphate (PIP2). No alteration of the alpha-adrenoreceptors was observed after 5 min of Ca2+-free perfusion. On the other hand, the observed changes in PLC activity during Ca2+-free perfusion appear to be due to some redistribution of the enzyme in the myocardium. These results suggest a possible role of the phosphoinositide/PLC pathway in the induction of Ca2+-paradox via mechanisms which do not appear to be associated with changes in the characteristics of alpha-adrenergic receptors. (Mol Cell Biochem121: 181–190, 1993) 相似文献
20.
The role of a transmembrane Ca2+ gradient in anion transport by Band 3 of human resealed erythrocyte ghosts has been studied. The results show that a transmembrane Ca2+ gradient is essential for the conformation of erythrocyte Band 3 with higher anion transport activity. The dissipation of the transmembrane Ca2+ gradient by the ionophore A23187 inhibits the anion transport activity. The extent of this inhibition approaches 90% as the Ca2+ concentration on both sides of the ghost membrane is increased to 1.0 mM and half-maximum inhibition is observed at 0.25 mM Ca2+. Addition of ATP (0.4 mM) to the resealing medium can partly reestablish the transmembrane Ca2+ gradient by activation of Ca2+-ATPase and alleviate the inhibition to some extent. N-ethylmaleimide, an inhibitor of erythrocyte Ca2+-ATPase, prevents such restoration. Electron micrographs reveal that numerous larger intramembranous particles can be observed on the P-faces of freeze-fractured resealed ghosts in the absence of a transmembrane Ca2+ gradient.Abbreviations DPA
dipicolinic acid
- EITC
eosin 5-isothiocyanate
- DIDS
4,4-diisothiocyanostilbene-2,2-disulfonate
- TES
N-Tris-(hydroxymethyl)methyl-2-aminoethane sulfonic acid
- PMSF
phenylmethyl-sulfonylfluoride
- NEM
N-ethylamaleimide
- BSA
bovine serum albumin
- EGTA
ethyleneglycol-bis (aminoethylether)-tetra-acetic acid
- EITC-Band 3
Band 3 labeled with EITC
- Cai
Ca2+ inside resealed ghosts
- Cao
Ca2+ outside resealed ghosts 相似文献