PubMed · 50843
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C W Haidle, J Bearden. 1975-08-04. Effect of bleomycin on an RNA-DNA hybrid.. https://doi.org/10.1016/s0006-291x(75)80458-x
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1. Lactate and O2 uptake and glucose output were studied in isolated livers from starved rats at perfusate flow rates varying from 100 to 7% of "normal" (11.25-0.75 ml/min per 100 g body wt.). 2. With moderate diminution of flow rate, lactate and oxygen uptake fell more slowly than would be expected if uptake purely depended on substrate supply. 3. Use of a mathematical model suggests that the intrinsic capacity of the liver for lactate uptake is unaffected until the flow rate falls below 25% of "normal". 4. Some lactate uptake was always observed even at 7% of the "normal" flow rate. 5. At flow rates below 33% of the "normal", lactate was increasingly metabolized by pathways other than gluconeogenesis, which became a progressively less important consumer of available O2. 6. ATP content decreased with diminution of flow rate, but substantially less markedly than did lactate uptake and glucose output. 7. Intracellular pH fell from a mean value of 7.25 at "normal" flow rate to 7.03 at 7% of the "normal" flow rate.
P1-(lin-Benzo-5'-adenosyl)-P5-(5'-adenosyl) penraphosphate and P1-(lin-benzo-5'-adenosyl)-P4-(5'-adenosyl) tetraphosphate have been synthesized from lin-benzoadenosine 5'-monophosphoromorpholidate and adenosine 5'-tetraphosphate and adenosine 5'-triphosphate. These mixed dinucleoside polyphosphates are potent inhibitors of porcine muscle adenylate kinase, with association constants of 2 x 10(5) M-1 for the pentaphosphate and 2 x 10(6) M-1 for the tetraphosphate, respectively, as determined by kinetics and fluorescence experiments. The increase in fluorescence intensities and fluorescence lifetimes of both inhibitors upon binding to adenylate kinase results from a breaking of the intramolecular stacking interaction observed when these ligands are free in solution and implicates their binding to the enzyme in an "open" or "extended" form. These results and the dimensional requirements of these inhibitors are discussed in relation to our current knowledge of the active site of adenylate kinase and to the known inhibitors of adenylate kinase, P1,P5-bis(5'-adenosyl) pentaphosphate and P1,P4-bis-(5'-adenosyl) tetraphosphate.
alpha-L-Glycerolphosphate dehydrogenase (sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase, EC 1.1.1.8) from Saccharomyces carlsbergensis was purified 400-fold. The enzyme preparation is free of interfering activities, such as glyceraldehyde phosphate dehydrogenase, alcohol dehydrogenase, triose phosphate isomerase and glycerolphosphatase. At pH 7.0 it is specific for NADH (Km = 0.027 mM with 0.8 mM dihydroxyacetone phosphate) and dihydroxyacetone phosphate (Km = 0.2 mM with 0.2 mM NADH). Between pH 5.0 and 6.0 the enzyme functions with NADPH, but only at 7% of the rate with NADH. Various anions (I- greater than SO42- greater than Br- greater than Cl-) act as inhibitors competing with the substrate dihydroxyacetone phosphate. Inorganic phosphate (Ki = 0.1 mM), pyrophosphate and arsenate are strong inhibitors. The nucleotides ATP and ADP are also inhibitory, but their action seems to be of the same type as the general anion competition (Ki = 0.73 mM for ATP). The results are consistent with the notion that the enzyme may regulate the redox potential of the NAD+/NADH couple during fermentation.