Adenine Diphosphate Research Articles

The effects of fasting on the concentrations of intermediate metabolites in the blood and hepatic tissues of pregnant and non-pregnant ewes

SummaryBlood and liver samples were taken from four fasted pregnant and five fasted non-pregnant Finnish Landrace × Dorset Horn ewes. The following metabolites were measured: adenine monophosphate (AMP), adenine diphosphate (ADP), adenine triphosphate (ATP), citrate, 2-oxoglutarate, phosphoenolpyruvate, pyruvate, lactate, 2-phosphoglycerate, 3-phosphoglycerate, α-glycerophosphate, malate, β-hydroxybutyrate, acetoacetate, glutamate, alanine and NAD+.The effects of a 6-day fast on non-pregnant ewes were shown as significant reductions in the hepatic concentrations of 2-phosphoglycerate, alanine, NAD+ and ADP, together with significant increases in the hepatic concentrations of 3-hydroxybutyrate, malate and the ratio of 3-hydroxybutyrate:acetoacetate. In the blood there were significant reductions in the concentrations of urea, citrate and in the ratio of 3-hydroxybutyrate: acetoacetate.Similar but more marked changes occurred in the late pregnant ewes, with additional significant reductions in the hepatic concentrations of citrate, ATP and the level of cell energy, and additional increases in the blood of the ratio of lactate: pyruvate and the concentrations of 3-hydroxybutyrate and 2-oxoglutarate. However, unlike the non-pregnant ewes no significant changes in either the plasma concentration of urea or the hepatic concentration of ADP were observed in the late pregnant ewes.

Concentrations of intermediate metabolites in the blood and hepatic tissues of pregnant and non-pregnant ewes

SummarySix late pregnant and six non-pregnant Finnish Landrace × Dorset Horn ewes were fed a standard diet. Blood and liver samples were taken and the concentrations of the following metabolites measured: adenine monophosphate (AMP), adenine diphosphate (ADP), adenine triphosphate (ATP), citrate, 2-oxoglutarate, phosphoenol-pyruvate, pyruvate, lactate, 2·phosphoglycerate, 3·phosphoglycerate, malate, β·hydroxybutyrate, acetoacetate, glutamate, alanine, NAD+ and NADH. Comparing non-pregnant with pregnant ewes the liver of the pregnant animals had reduced concentrations of lactate, ADP, NAD+ and NADH, and in the blood there were reductions in lactate, pyruvate, lactate/pyruvate ratio and urea. The concentrations of the other metabolites of the pregnant ewes receiving adequate nutrition were little changed from those of the non-pregnant ewes. The significance of these findings is discussed.

Two-step binding of adenosine diphosphate to L-glutamate dehydrogenase. Effect on the binding of reduced nicotinamide adenine diphosphate and on enzymatic catalysis.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTTwo-step binding of adenosine diphosphate to L-glutamate dehydrogenase. Effect on the binding of reduced nicotinamide adenine diphosphate and on enzymic catalysisAlan H. Colen, Dallas G. Cross, and Harvey F. FisherCite this: Biochemistry 1974, 13, 11, 2341–2347Publication Date (Print):May 1, 1974Publication History Published online1 May 2002Published inissue 1 May 1974https://doi.org/10.1021/bi00708a016RIGHTS & PERMISSIONSArticle Views53Altmetric-Citations29LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (807 KB) Get e-Alerts Get e-Alerts

Value of adenine, various nucleosides, and ouabain in maintenance of integrity of red blood cells under blood bank conditions.

Summary. The effects of adenine and various nucleosides on adenine nucleotide metabolism in red cells, as well as on other factors related to the storability of blood were compared during six weeks of storage under blood bank conditions. Adenosine triphosphate (ATP) and total adenine nucleotides were maintained at higher levels, and higher ratios of ATP to adenine diphosphate were observed, in blood containing citrate‐phosphate‐dextrose (CPD) solution than in blood containing acid‐citrate‐dextrose (ACD) solution. Higher levels of ATP and total adenine nucleotides were maintained in blood containing ACD together with both adenine and inosine than in blood containing ACD alone or together with only one of the two purines. ACD‐adenine was more effective in maintaining adenine nucleotides than was ACD‐inosine. Addition of uridine did not have any effect on adenine nucleotides in red cells. ATP and total adenine nucleotides were maintained at higher levels in CPD‐adenine than in CPD alone. The effect of CPD‐inosine or CPD‐adenine‐inosine was not investigated. ACD‐inosine caused a marked increase in plasma lactate, and inhibited glucose utilization, during storage. An increase in plasma inorganic phosphate was delayed by the addition of inosine, and this effect was augmented by adenine and guanosine. There were no findings suggestive of a beneficial effect of these additives on active cation transport, osmotic fragility, hemolysis, or the deterioration of blood cell morphology. Ouabain, an inhibitor of ATPase, had little effect on red cell nucleotide patterns or on other biochemical or morphological criteria for blood storage, possibly because of the low activity of ATPase at 4°C.

Fractionation and Characterization of the Plasma and Mesosome Membrane of Listeria monocytogenes

Protoplasts of Listeria monocytogenes strain 42 were fractionated after control lysis on a Ficoll (a polysucrose) density gradient. Visually, five zones could be recognized in the gradient. The first one was composed of amorphous cytoplasmic solutes (fraction 1a) and a mixture of particles (fraction 1b). These were: (i) light particles that were lipase-sensitive and composed of six subunits and (ii) heavy particles, sensitive to ribonuclease and devoid of fine structure. The second zone consisted of tubules and vesicles still harboring cytoplasmic components (fraction 2), whereas the third zone contained only empty vesicles and protoplast ghosts (fraction 3). The material congregating into the fourth zone was morphologically identical to that of the third (fraction 3a). The fifth and heaviest zone contained a mixture of (i) particles without any substructure and (ii) partly lysed protoplasts (fraction 4). Fractions 1b and 4 were the richest in nucleic acids (ribonucleic acid, 11.4 and 9.4%, respectively; deoxyribonucleic acid, 5.1 and 4.8%, respectively), whereas fraction 1b had the highest protein contents (74.6%). Phospholipids were mainly found in fractions 2 and 3. Except for fraction 1, all materials contained significant amounts of protein-bound phosphorus. The main concentrations of four enzymes were: glucose-6-phosphate dehydrogenase (fraction 1a); adenosine triphosphatase and reduced nicotinamide adenine diphosphate oxidase (fraction 3); nitro blue tetrazolium chloride reductase (fraction 2). Fractionation of strain 42 after addition of (32)P during the mid-log phase of growth revealed that the radio-activity was mainly detected in fraction 1b, when growth in the presence of the marker was allowed for 10 min, and in fraction 2, when growth was allowed for 90 min. The vesicles of fraction 2, often tubular, are probably of mesosomal origin, whereas those of fraction 3, which are always spherical, represent, most likely, the bulk of the cell plasma membrane. Our data showed slight chemical differences between these two fractions, but the differences in enzymatic activities and lipid-phosphorus incorporation during long pulse experiments were most dramatic.

Optimal concentration of nicotinamide adenine diphosphate in pyruvate assays.

Optimal concentration of nicotinamide adenine diphosphate in pyruvate assays.