Adenosine Triphosphate/adenosine Diphosphate Research Articles

Glucose-stimulated signaling pathways in biphasic insulin secretion.

Glucose-stimulated biphasic insulin secretion involves at least two signaling pathways, the KATP channel-dependent and KATP channel-independent pathways, respectively. In the former, enhanced glucose metabolism increases the cellular adenosine triphosphate/adenosine diphosphate (ATP/ADP) ratio, closes KATP channels and depolarizes the cell. Activation of voltage-dependent Ca(2+) channels increases Ca(2+) entry and [Ca(2+)]i and stimulates insulin release. The KATP channel-independent pathways augment the response to increased [Ca(2+)]i by mechanisms that are currently unknown. However, they affect different pools of insulin-containing granules in a highly coordinated manner. The beta-cell granule pools can be minimally described as reserve, morphologically docked, readily and immediately releasable. Activation of the KATP channel-dependent pathway results in exocytosis of an immediately releasable pool that is responsible for the first phase of glucose-stimulated insulin release. Following glucose metabolism, the rate-limiting step for the first phase lies in the rate of signal transduction between sensing the rise in [Ca(2+)]i and exocytosis of the immediately releasable granules. The immediately releasable pool of granules can be enlarged by previous exposure to glucose (by time-dependent potentiation, TDP), and by second messengers such as cyclic adenosine monophosphate (cyclic AMP) and diacylglycerol (DAG). The second phase of glucose-stimulated insulin secretion is due mainly to the KATP channel-independent pathways acting in synergy with the KATP channel-dependent pathway. The rate-limiting step here is the conversion of readily releasable granules to the state of immediate releasability, following which, in an activated cell they will undergo exocytosis. In the rat and human beta-cell the KATP channel-independent pathways induce a time-dependent increase in the rate of this step that results in the typical rising second-phase response. In the mouse beta-cell the rate appears not to be changed much by glucose. Potential intermediates involved in controlling the rate-limiting step include increases in cytosolic long-chain acyl-CoA levels, adenosine triphosphate (ATP) and guanosine triphosphate (GTP), DAG binding proteins, including some isoforms of protein kinase (PKC), and protein acyl transferases. Agonists that can change the rate-limiting steps for both phases of insulin release include those like glucagon-like peptide 1 (GLP-1) that raise cyclic AMP levels and those like acetylcholine that act via DAG.

Polyene antibiotics: Relative degrees of in vitro cytotoxicity and potential effects on tubule phospholipid and ceramide content

Polyene antibiotic administration is limited by dose-dependent nephrotoxicity. The latter is believed to be mediated by polyene anchoring to plasma membrane cholesterol, resulting in pore formation, abnormal ion/solute flux, adenosine triphosphate (ATP) declines, and, ultimately, a loss of tubule viability. The relative nephrotoxicity of these agents and their liposomal preparations has remained poorly defined. Thus, freshly isolated mouse proximal tubules or cultured human proximal tubule (HK-2) cells were exposed to either nystatin, amphotericin B, or three different polyene liposomal preparations (Nyotran, AmBisome, or Abelcet; 4 to 64 μg/mL). The impact of these agents on (1) plasma membrane injury (sodium-driven ATP consumption, assessed by ATP–adenosine diphosphate [ADP] ratios); (2) cellular susceptibility to superimposed injury (chemical hypoxia or ferrous ammonium sulfate–mediated oxidative stress; assessed by lactate dehydrogenase release); and (3) membrane cholesterol, phospholipid, and ceramide expression was assessed. Amphotericin B was more cytotoxic than nystatin (~25% to 50% greater ATP-ADP ratio declines). Most of this toxicity could be eliminated by polyene liposomal formulation. Nevertheless, the liposomal polyenes still fully sensitized tubule cells to superimposed chemical hypoxic (antimycin/deoxyglucose), but not oxidant, attack. Nystatin and amphotericin B caused acute increments in tubule sphingomyelin-phosphatidylcholine ratios and ceramide content (indicating an impact on the plasma membrane extending beyond the classic view of pore formation with ion flux). In conclusion, (1) nystatin is seemingly less cytotoxic than amphotericin B (in contrast to the prevailing clinical view); (2) liposomal formulation markedly decreases this cytotoxicity; (3) despite this reduced toxicity, liposomal polyenes are still able to render tubule cells more vulnerable to selected forms of superimposed injury; and (4) acute alterations in plasma membrane phospholipid and ceramide expression are previously unrecognized consequences and potential mediators of polyene-mediated tubular cell attack.

Heart failure: is there an energy deficit contributing to contractile dysfunction?

Alterations in myocardial energy metabolism have been demonstrated in both animal experiments and clinical observations. Whether these changes contribute to heart failure has been a longstanding and controversial issue. I. The creatine kinase (CK) system and the high energy phosphates under physiological conditions and in acute heart failure: 1. According to in vivo and in vitro experiments the myocardial creatine/creatine phosphate (Cr/CP) system is directly linked to mitochondrial oxidative phosphorylation via the mitochondrial CK. 2. The shift in the mass action ratio of the CK reaction with increasing myocardial oxygen consumption enables marked stimulation of mitochondrial respiratory function via the Cr/CP system with almost maintained free energy of the adenosine triphosphate/adenosine diphosphate (ATP/ADP) system. 3. In acute heart failure the depressed myocardial content mainly of CP can be considered as an adaptive mechanism related to increased oxygen demands. II. The CK system and the high energy phosphates in chronic heart failure: 1. The alterations observed in the CK system in chronic heart failure cannot be interpreted in terms of an "energy deficit" (i.e., the excess of what is spent over what is received on energy). 2. "Energy reserve" (i.e., energy kept back for future use, to fill an emergency) is markedly reduced in heart failure. 3. Under steady state conditions decreased "energy reserve" cannot be expected to contribute to heart failure. Under stress conditions, however, this mechanism is manifest by reducing contractile reserve. 4. The mechanisms by which decreased "energy reserve" induces depression of contractile reserve is not elucidated. III. Heart failure related to alterations in energy metabolism (mitochondrial diseases, stunned, and hibernating myocardium): 1. The phenotype of mitochondrial diseases is predominantly determined by neurological disorders and myopathies. Therefore, the patients are rarely referred to a cardiologist, although the cardiac involvement may ultimately determine the patients' prognosis. 2. Stunned and hibernating myocardium are characterized by prolonged contractile dysfunction in the presence of reversibly damaged myocardium. The underlying mechanisms and its triggers are unknown. 1. The reduced energy reserve in heart failure may be considered to contribute to the progression of the disease. 2. As an alternative, however, it can likewise represent a mechanism to protect the endangered myocardium from overload.

Metabolic adaptations by the leech Nephelopsis obscura during long‐term anoxia and recovery

AbstractMetabolic adaptations to long‐term (40 day) anoxia were determined in two size groups (small and large) of the freshwater leech Nephelopsis obscura. Neither size group accumulated the lactic acid during anoxia; rather succinate and alanine were the major end products. Glycogen and amino acids were the primary energy reserves utilized with lipid also utilized by small N. obscura. After 40 days of anoxia glycolytic flux was reduced by 99.8% in small and 99.7% in large N. obscura. Cellular energy status adenosine triphosphate/adenosine diphosphate (ATP/ADP) also declined significantly in small (79%) and large (69%) leeches. After return to normoxia the energy charge in small N. obscura was restored within 6 hours and glycogen, malate, succinate, alanine, and aspartate restored within 24 hours. Large N. obscura utilized lower proportions of their energy reserves than small N. obscura. © 1993 Wiley‐Liss, Inc.

31P-nuclear magnetic resonance evidence of abnormal skeletal muscle metabolism in patients with chronic lung disease and congestive heart failure

The development of 31P-nuclear magnetic resonance (NMR) has enabled direct and non-invasive measurements of muscle metabolism. Serial measurements of the phosphocreatine/inorganic phosphate (PCr/Pi) ratio, which is closely related to the adenosine triphosphate/adenosine diphosphate (ATP/ADP) ratio and pH during and after forearm exercise were performed in 11 patients with chronic lung disease (CLD), nine patients with chronic heart failure (CHF) and eight control subjects. As compared with control subjects, the PCr/Pi ratio in the patients with CLD or CHF was lower during the recovery period and significantly lower at three and 4 min exercise. The pH values after exercise were lower in patients with CLD or CHF compared to control subjects. The PCr/Pi ratio at 4 min after exercise in the patients with CLD or CHF did not correlate with parameters of cardiac function or arterial and mixed venous oxygen tension. The arterial oxygen content and output in patients with CLD and CHF were significantly lower than that of control subjects. Nutritional parameters were not statistically different among the three groups. These observations suggest that metabolic abnormalities may be present in the skeletal muscles of patients with CLD and CHF that are not due to under-nutrition. These may result from reduced arterial oxygen output and, partially, from physical detraining.

Effects of Halothane and Decreased PO2 on High Energy Phosphate Levels Maintained by Isolated Rat Liver Mitochondria

Steady states of oxidative phosphorylation were achieved in mitochondrial suspensions continuously equilibrated with constant gas mixtures, simulating the conditions under which mitochondria contribute to the cellular energy status in vivo. The dependence of the mitochondria-maintained adenosine triphosphate/adenosine diphosphate (ATP/ADP) ratio on oxygen and halothane levels was examined at predetermined, clinically relevant concentrations of both gases. Inclusion of 1% halothane in the gas mixture decreased ATP/ADP by about half when mitochondrial respiration was supported by NAD-linked substrate (glutamate); succinate-supported ATP/ADP was not inhibited. With either substrate, and whether or not 1% halothane was present. ATP/ADP was unaffected by decreases in PO2 to values as low as 1.6 mm Hg. Under a range of typical in vivo conditions, therefore, 1% halothane significantly inhibited the mitochondrial contribution to steady state energy balance, whereas decreases in PO2 did not. Combined effects of 1% halothane and reduced PO2 on ATP/ADP were not seen, i.e., halothane did not increase the critical PO2 level (hypoxic threshold) for inhibition of mitochondrial ATP production.

Energy deficits in hepatocytes isolated from phenobarbital-treated or fasted rats and briefly exposed to halothane and hypoxia in vitro.

Experimental factors implicated in the pathogenesis of halothane hepatotoxicity in the phenobarbital-hypoxia rat model were examined for direct effects on the energy status of isolated rat liver cells in vitro. Intact hepatocytes were isolated after collagenase perfusion of livers of adult male Fischer 344 rats previously treated with phenobarbital (0.1% in drinking water for 5-7 days) and/or deprived of food for 48 h. Cells were incubated in Krebs-Henseleit buffer + substrates for 10 min at steady states of energy metabolism, with extracellular PO2 constant at 32, 16, or 4 mmHg +/- 1% halothane. Fasting produced the largest energy deficits in incubated hepatocytes, regardless of phenobarbital treatment status, PO2 value, or presence/absence of halothane. The combination of hypoxic PO2 (4 mmHg) and 1% halothane shifted lactate metabolism toward lactate production, whereas hypoxia or halothane alone did not. Prior phenobarbital treatment plus hypoxia decreased adenosine triphosphate/adenosine diphosphate (ATP/ADP) and increased lactate production compared with drug treatment or hypoxia alone. We conclude that pathogenic factors that interact to produce halothane hepatotoxicity act directly and jointly on isolated liver cells to produce energy deficits within 10 min. Differences in the relative importance of pathogenic factors in vitro and in vivo suggest that short-term, direct effects on hepatocellular energy status are not solely responsible for halothane hepatotoxicity.

Effects of fenvalerate on biochemical parameters, survival, and reproduction of Daphnia magna

Daphnia magna were exposed to fenvalerate at nominal concentrations of 0.5, 0.25, 0.13, 0.06, and 0.03 μg/liter for 21 days. On Days 7 and 21 of exposure, levels of ribonucleic acid (RNA), deoxyribonucleic acid (DNA), adenosine diphosphate (ADP), adenosine triphosphate (ATP), glycogen, and lipid were measured, and the results were related to survival and reproduction during the 21-day test period. Survival was not significantly ( α = 0.05) affected by the 21-day exposure; however, reproduction was reduced at fenvalerate concentrations of 0.25 and 0.5 μg/liter. On Day 7, protein, RNA, ADP, caloric equivalents, and glycogen were also significantly reduced at fenvalerate concentrations of 0.25 and 0.5 μg/liter. Thus, these biochemical parameters identified the same no observable effect concentration (NOEC) as did reproduction. Variables derived from biochemical parameters were related to reduced protein growth and reproduction. Decreases in protein/RNA and glycogen/lipid ratios and increases in ADP DNA , ADP ATP , protein/RNA/DNA, and lipid/DNA ratios were observed at Day 7 for those daphnia exposed to 0.5 μg/liter of fenvalerate. The only derived variable that reflected the reduced protein growth at Day 7 in daphnia exposed to 0.25 μg/liter of fenvalerate was the glycogen/lipid ratio. Biochemical determinations at Day 21 indicated that the organisms exposed to 0.25 μg/liter of fenvalerate were not different from controls, whereas those exposed to 0.5 μg/liter were still affected.

48] Fluorescent nucleotide analogs as active site probes for the ADP/ATP carrier and the uncoupling protein

Publisher Summary This chapter focuses on the fluorescent nucleotide analogs as active site probes for the adenosine diphosphate (ADP)/ adenosine triphosphate (ATP) carrier and the uncoupling protein. The 1,5- dimethylaminonaphthoyl (DAN) derivatives DAN-adenine monophosphate (AMP), DAN-ADP, and DAN-ATP have identical fluorescence properties. Their fluorescence is virtually quenched in aqueous solution, whereas a high fluorescence yield is obtained in nonaqueous media, such as dioxane and ethanol. The DAN-nucleotides added to rat liver mitochondria do not give a marked fluorescence. In beef heart mitochondria, they exhibit a relatively small signal which is fully enhanced in submitochondrial (sonic) particles. Also breaking the mitochondria by freezing-thawing or by detergents enhances the fluorescence response. The DAN-nucleotides bind also to the soluble and partially purified ADP/ATP carrier (AAC) with a fluorescence maximum at a slightly longer wavelength, 519 Nm. In the solubilized AAC, the full fluorescence response to addition of DAN-AMP is observed only in the presence of ADP or ATP. This is interpreted to show that the AAC is, from the start, partially in the m-state and partially in the c-state. Only when the substrates for the ADP–ATP transport are provided the transition between the c- and m-state can be accomplished since the unloaded carrier cannot undergo this transition. Thus the carrier population in the c-state is largely converted into the m-state under the pulling force of the DAN-AMP binding.

Some thoughts on the evolutionary basis for the prominent role of ATP and ADP in cellular energy metabolism

The predominance of the adenosine triphosphate/adenosine diphosphate (ATP/ADP) couple in cellular phosphorylation reactions, including those that form the basis for cellular energy metabolism, cannot be explained on thermodynamic grounds since a variety of "high energy phosphate" compounds (including ADP itself) found in the cell would, based on thermodynamic considerations, be at least as effective as ATP in serving as a phosphoryl donor. How then did present-day organisms come to rely on the ATP/ADP couple as the principal mediator of phosphorylation reactions? The early appearance of adenine compounds in the prebiotic environment is suggested by experiments indicating that, relative to other purine or pyridimine compounds, adenine derivatives are preferentially synthesized under simulated prebiotic conditions (Ponnamperuma et al., 1963). In addition to the roles of adenine nucleotides in phosphorylation reactions, other adenine derivatives (e.g. Coenzyme A, flavin adenine dinucleotide, puridine nucleotides) are employed in a variety of metabolic roles. The principal function of the adenine moiety in these latter cases is in the binding of these derivatives to the relevant enzyme. The capability for binding of the adenine moiety appears to have arisen early in evolution and been exploited in a multitude of contexts, a suggestion consistent with observed similarities between the binding sites of several enzymes employing adenine derivatives as substrate. The early availability of suitable adenine compounds in the biosphere and development of complementary binding sites on cellular proteins, coupled with the expected advantages in having a limited number of metabolites as central mediators of endergonic and exergonic metabolism could readily have led to the observed pre-eminence of adenine nucleotides in cellular energy metabolism.(ABSTRACT TRUNCATED AT 250 WORDS)

Additional effects of monovalent cations on the lysine-sensitive aspartokinase of E. coli B

The apparent specificity of activation of lysine-sensitive aspartokinase (E.C.2.7.2.4) from E. coli by monovalent cations differs depending on the assay used and on the Mg 2+ concentration. Activity is nearly absolutely dependent on and is highly specific for a monovalent cation in the aspartate semialdehyde dehydrogenase coupled assay or the adenosine triphosphate-adenosine diphosphate exchange assay. Little specificity for monovalent cations is observed using the aspartyl hydroxamate assay. Activation and specificity are also altered by Mg 2+ concentrations at a constant 5 mM nucleotide concentration. At a low ( 1.25 or 1.6 mM) Mg 2+ concentration, monovalent cation activation and specificity are nearly absolute. Less dependence on monovalent cations and less specificity are observed at a higher Mg 2+ concentration (6 mM). Li + inhibits aspartokinase competitively with respect to either K + or NH 4 +. Monovalent cations are also thermoprotective and differential thermal inactivation experiments at 56°C reveal that NH 4 + and K +, either of which will produce maximum catalytic activity, interact differently with aspartokinase. K + interacts with positive cooperativity, whereas NH 4 + does not. K +, NH 4 +, and Na + are about equally effective in enhancing the dissociation of the aspartokinase-aspartylphosphate complex. Li + is less effective.

Effects of arginine and some analogues of the partial adenosine triphosphate-adenosine diphosphate exchange reaction catalysed by arginine kinase. Evolutionary divergence in the mechanism of action of a monomer and a dimer arginine kinase

1. Both the monomer arginine kinase from lobster muscle and the dimer arginine kinase from Holothuria forskali catalyse the ATP-ADP partial exchange reaction at rates equal to 3 and 0.6% of the normal rate of transphosphorylation respectively. The Mg2+-nucleotide complex is the substrate for this as it is for the kinase reaction. 2. Analogues of arginine inhibit the exchange reaction of the lobster enzyme but enhance that of the Holothuria enzyme. 3. With the lobster enzyme NO3- has no effect on the exchange reaction alone and inhibit only slightly the apparent enhancement of the exchange reaction produced by the addition of arginine. This is compatible with previous findings for this enzyme that formation of the anion-stabilized dead-end complex, enzyme-arginine-MgADP-NO3-, does not occur to any marked degree. 4. About 80% of the ADP-ATP exchange reaction of the lobster enzyme remains after inhibition with iodoacetamide. This is further decreased to 65% by the addition of L-arginine, indicating that this substrate does bind to the thiolmodified enzyme. 5. It is concluded that the partial exchange reaction is a genuine phenomenon not mediated by trace amounts of arginine. From the effects of arginine and related compounds it would appear that during the normal kinase reaction the partial ATP-ADP exchange reaction is suppressed in the lobster enzyme but enhanced in the Holothuria enzyme. This reflects a remarkable evolutionary divergence of two homologous enzymes.

Effects of laser photocoagulation on adenine nucleotides in rabbit retinas.

High-pressure liquid chromatography was used to provide a qualitative biochemical assessment of laser effects on retinal metabolism. The adenosine triphosphate-adenosine diphosphate ratio and the Atkinson energy charge are considerably increased in laser-treated rabbit retinas compared to the contralateral untreated retinas.

Is the Adenosine Diphosphate-Adenosine Triphosphate Translocase System Influenced by Mitochondrial Genes?

Is the Adenosine Diphosphate-Adenosine Triphosphate Translocase System Influenced by Mitochondrial Genes?

Energy dependent changes in the cytochromes of the mitochondrial respiratory chain

In intact mitochondria a stoichiometric coupling exists between cytochrome a 3 and the hydrolysis of adenosine triphosphate (ATP). In each case the modification of one cytochrome a 3 (measured as a spectral change) is coupled to the hydrolysis of one ATP molecule. When both cytochromes a 3 and a are reduced the measured equilibrium constant is 0.06 m −1 but this constant is 10 3 M −1 when both cytochromes are oxidized. When the sixth ligand for cytochrome a 3 is an externally added ligand (HCN, H 2S, CO, NO) the equilibrium constant is different for each ligand, suggesting that the ATP induced modification is of the fifth ligand but that it is energetically dependent on the chemical nature of the sixth ligand. The measured half-reduction potentials for cytochromes a 3 and b T are dependent on the concentrations of added ATP, adenosine diphosphate (ADP), and orthophosphate. The relationship is consistent with a ligand exchange mechanism in which the ligand on the cytochrome is dependent on the phosphate potential ( ATP ADP × P i). The equilibrium constants obtained by the ligand exchange treatment of the E m values for cytochrome a 3 are consistent with those obtained by direct measurement of the equilibrium constants for the spectrally measured changes.

Effects of cations on the adenosine diphosphate-adenosine triphosphate exchange reaction catalyzed by rat brain microsomes

Some properties of a (Na + + Mg 2+)-dependent ADP-ATP exchange reaction catalyzed by Nal-treated rat brain microsomes have been investigaged. The (Na + + Mg 2+)-activated exchange exhibited an absolute requirement for Na +, was inhibited by ouabain and stimulated 2–3-fold by oligomycin. The optimum MgCl 2 concentration for the (Na + + Mg 2+)-activated exchange was 1.0 mM, but in the presence of oligomycin 3.0 mM MgCl 2 was required for optimum activity. The exchange reaction exhibited a complex multiphasic response to increasing concentration of Na +, with activity increasing up to 200 mM NaCl.

Effect of Potassium on Sodium-dependent Adenosine Diphosphate-Adenosine Triphosphate Exchange Activity in Kidney Microsomes

Abstract Maximal activation of a Na+-dependent adenosine diphosphate-adenosine triphosphate exchange reaction mediated by kidney microsomes was achieved at 0.1 mm and 0.4 mm Mg++ in the presence of 1.5 mm and 32 mm Na+, respectively. K+ inhibited the Na+-dependent exchange rate when lower concentrations of Na+ and Mg++ were used and stimulated it in the presence of 0.4 mm Mg++ and 32 mm Na+. The inhibitory effect of K+ could be reversed either by increasing the Na+ concentration or decreasing that of K+. N-Ethyl-maleimide treatment of microsomes abolished the stimulatory effect of K+. Ouabain, alkaline pH, and lower temperatures less effectively decreased stimulation of Na+-dependent exchange by K+. Mg++ and K+ appeared to exhibit competitive antagonism on (Na+ + K+)-sensitive transphosphorylation activity. It is proposed that the stimulation of Na+-dependent adenosine diphosphate-adenosine triphosphate exchange reaction by K+ may be mediated, in part, by slowing the conversion of one form of the phosphoenzyme E1-P into another E2-P.

Potassium ion-stimulated and sodium ion-dependent adenosine diphosphate-adenosine triphosphate exchange activity in a kidney microsomal fraction.

1. K(+) did not affect the Mg(2+)-dependent transphosphorylation but markedly increased the Na(+)-stimulated ADP-ATP exchange rate mediated by a microsomal fraction from guinea-pig kidney. 2. Rb(+), Cs(+), NH(4) (+) and Li(+) were equally effective in stimulating the Na(+)-dependent ADP-ATP exchange activity. 3. Treatment of the microsomal fraction with N-ethylmaleimide or increased concentrations of Mg(2+) prevented stimulation of the Na(+)-dependent exchange reaction by K(+). 4. Ouabain (2.5mum) inhibited ATP hydrolysis by 33% but did not decrease the K(+)-stimulated Na(+)-dependent ADP-ATP exchange rate. 5. A possible mechanism for stimulation of exchange activity by K(+) is discussed.

Antimycin A Stimulation of Rate-limiting Steps of Photosynthesis in Isolated Spinach Chloroplasts

Changes in levels of metabolites in isolated spinach (Spinacia oleracea) chloroplasts seen upon addition of antimycin A suggest that the activities of enzymes mediating several regulated reactions are affected. Apparently, the presence of added antimycin A does not increase the level of CO(2) in the chloroplasts, nor does it stimulate CO(2) fixation by increasing the level of the carboxylation substrate, ribulose-1,5-diphosphate. Rather, it appears that antimycin A increases CO(2) fixation rate by indirectly stimulating the enzyme, ribulose-1,5-diphosphate carboxylase (E.C. 4.1.1.39), which mediates the carboxylation of ribulose-1,5-diphosphate to give 3-phosphoglycerate. Another rate-limiting enzyme of the reductive pentose phosphate cycle, hexose diphosphatase (E.C. 3.1.3.11), seems also to be stimulated. The synthesis of polysaccharides (mostly starch) seems also to be stimulated. These results are interpreted as indicating that antimycin A addition enhances the general activation of those enzymes which already are activated during photosynthesis but are inactive in the dark. The ratio of adenosine triphosphate-adenosine diphosphate under conditions of photosynthesis was only moderately decreased in the presence of antimycin A, perhaps accounting in part for an observed increase in accumulation of 3-phosphoglycerate as compared with dihydroxyacetone phosphate. No significant effect on movement of metabolites from the chloroplast to the medium was seen.

On the role of the adenosine diphosphate-adenosine triphosphate exchange reaction in oxidative phosphorylation: Effect of calcium

FEBS LettersVolume 7, Issue 4 p. 339-342 Full-length articleFree Access On the role of the adenosine diphosphate-adenosine triphosphate exchange reaction in oxidative phosphorylation: Effect of calcium F.L. Bygrave, F.L. Bygrave Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this authorK.C. Reed, K.C. Reed Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this author F.L. Bygrave, F.L. Bygrave Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this authorK.C. Reed, K.C. Reed Department of Biochemistry, The Australian National University, Faculty of Science, Canberra, A.C.T., AustraliaSearch for more papers by this author First published: May 01, 1970 https://doi.org/10.1016/0014-5793(70)80200-9Citations: 9AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 F.L. Bygrave, A.L. Lehninger, J. Biol. Chem., 241, (1966), 3894– 2 F.L. Bygrave, K.C. Reed, Proc. Australian Biochem. Soc., (1969), 59– 3 C. Schnaitman, P.L. Pederson, Biochem. Biophys. Res. Commun., 30, (1968), 428– 4 W.C. Schneider, J. Biol. Chem., 176, (1948), 259– 5 J.F. Morrison, Anal. Biochem., 24, (1968), 106– 6 R.J.L. Allen, Biochem. J., 34B, (1940), 858– 7 F.L. Bygrave, unpublished observations. 8 A.L. Lehninger, The Mitochondrion (1963), Benjamin New York 95– 9 E. Racker, Mechanisms in Bioenergetics (1965), Academic Press New York 129– 10 M.G. Colomb, J.G. Laturaze, P.V. Vignais, Biochem. Biophys. Res. Commun., 24, (1966), 909– 11 R.P. Glaze, C.L. Wadkins, J. Biol. Chem., 242, (1967), 2139– 12 A. Goffeau, P.L. Pederson, A.L. Lehninger, J. Biol. Chem., 242, (1967), 1815– 13 G.S.P. Groot, S.G. van den Bergh, Biochim. Biophys. Acta, 153, (1968), 22– 14 M.E. Pullman, H.S. Penefsky, A. Datta, E. Racker, J. Biol. Chem., 235, (1960), 3322– 15 H. Zalkin, M.E. Pullman, E. Racker, J. Biol. Chem., 240, (1965), 401– 16 F.L. Bygrave, A.L. Lehninger, Proc. Natl. Acad. Sci., 51, (1967), 1409– 17 P. Mitchell, Biol. Rev., 41, (1966), 445– 18 P.L. Pederson, C. Schnaitman, J. Biol. Chem., 244, (1969), 5065– 19 S.O. Nielson, A.L. Lehninger, J. Biol. Chem., 215, (1955), 555– Citing Literature Volume7, Issue4May 01, 1970Pages 339-342 ReferencesRelatedInformation