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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The phosphorylated form of liver glycogen phosphorylase (alpha-1,4-glucan : orthophosphate alpha-glucosyl-transferase, EC 2.4.1.1) (phosphorylase a) is active and easily measured while the dephosphorylated form (phosphorylase b), in contrast to the muscle enzyme, has been reported to be essentially inactive even in the presence of AMP. We have purified both forms of phosphorylase from rat liver and studied the characteristics of each. Phosphorylase b activity can be measured with our assay conditions. The phosphorylase b we obtained was stimulated by high concentrations of sulfate, and was a substrate for muscle phosphorylase kinase whereas phosphorylase a was inhibited by sulfate, and was a substrate for liver phosphorylase phosphatase. Substrate binding to phosphorylase b was poor (KM glycogen = 2.5 mM, glucose-1-P = 250 mM) compared to phosphorylase a (KM glycogen = 1.8 mM, KM glucose-1-P = 0.7 mM). Liver phosphorylase b was active in the absence of AMP. However, AMP lowered the KM for glucose-1-P to 80 mM for purified phosphorylase b and to 60 mM for the enzyme in crude extract (Ka = 0.5 mM). Using appropriate substrate, buffer and AMP concentrations, assay conditions have been developed which allow determination of phosphorylase a and 90% of the phosphorylase b activity in liver extracts. Interconversion of the two forms can be demonstrated in vivo (under acute stimulation) and in vitro with little change in total activity. A decrease in total phosphorylase activity has been observed after prolonged starvation and in diabetes.
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PMID:Characteristics of the dephosphorylated form of phosphorylase purified from rat liver and measurement of its activity in crude liver preparations. 0 75

The intracellular levels of glutamine synthetase (GS) in Anacystis nidulans grown under different conditions were determined using a whole-cell assay. Nitrate-grown cells have 64% more GS than cells grown in ammonium sulfate. Nitrogen starvation does not affect GS levels appreciably. Incubation of nitrate-grown cells with ammonium sulfate does not change the ratio of gamma-glutamyl transferase activities stimulated by Mg2+ and Mn2+ ions. An in vitro test of adenylylation indicates that algae do not have an endogenous adenylyl transferase (ATase) and that algal GS is not adenylylatable by the Klebsiella aerogenes ATase. Some characteristics of the GS-membrane complex were determined by centrifugation of the complex under varying conditions of pH and ionic strength. In this way, it was shown that acid pH (4.5) stabilizes the complex and high ionic strength tends to solubilize the enzyme. A simple partial purification of GS (89-fold) was developed based on the sedimentation properties of GS.
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PMID:Distinctive properties of glutamine synthetase from the cyanobacterium Anacystis nidulans. 3 92

Male rabbits were injured by a single mechanical dilatation injury of aorta and then injected with prednisone 2 mg/kg or saline for 14 days or subjected to starvation. The biosynthesis of the sulfated glycosaminoglycans as evaluated by the uptake of 35S-sulfate and the content of the glycosaminoglycans were measured on the intima-media layer of the descending thoracic aorta. The results indicate that prednisone may inhibit the biosynthesis of heparan and/or dermatan sulfate while starvation increases the biosynthesis of all the sulfated glycosaminoglycans. No alterations were observed in the total amount of glycosaminoglycans in aorta following glucocorticoid injection or starvation. The metabolism of aortic glycosaminoglycans during repair is less sensitive to the action of prednisone than in undamaged aorta. This contrasts with the effect of prednisone on the metabolism of aortic collagen.
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PMID:Glucocorticoid and starvation effect on glycosaminoglycans in vascular connective tissue. Biochemical studies on repair processes in rabbit aorta. 13 64

The rate of transport of L-amino acids by Saccharomyces cerevisiae epsilon 1278b increased with time in response to nitrogen starvation. This increase could be prevented by the addition of ammonium sulfate or cycloheximide. A slow time-dependent loss of transport activity was observed when ammonium sulfate (or ammonium sulfate plus cycloheximide) was added to cells after 3 h of nitrogen starvation. This loss of activity was not observed in the presence of cycloheximide alone. In a mutant yeast strain which lacks the nicotinamide adenine dinucleotide phosphate-dependent (anabolic) glutamate dehydrogenase, no significant decrease in amino acid transport was observed when ammonium sulfate was added to nitrogen-starved cells. A double mutant, which lacks the nicotinamide adenine dinucleotide phosphate-dependent enzyme and in addition has a depressed level of the nicotinamide adenine dinucleotide-dependent (catabolic) glutamate dehydrogenase, shows the same sensitivity to ammonium ion as the wild-type strain. These data suggest that the inhibition of amino acid transport by ammonium ion results from the uptake of this metabolite into the cell and its subsequent incorporation into the alpha-amino groups of glutamate and other amino acids.
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PMID:Inhibition of amino acid transport by ammonium ion in Saccharomyces cerevisiae. 24 Aug 6

Molybdate and selenate are structural analogs of sulfate that inhibit synthesis of adenosine 5'-phosphosulfate by ATP sulfurylase (sulfate adenylyltransferase, ATP:sulfate adenylyltransferase, EC 2.7.7.4) in crude extracts of tobacco XD cells. Both of these anions derepress ATP sulfurylase in cells growing on sulfate, but not in cells growing on L-cysteine. However, the two anions appear to derepress by different mechanisms. Molybdate caused derepression only at concentrations that were in excess over sulfate and were sufficient to inhibit growth and protein accumulation, indicating that the derepression resulted from sulfur starvation. Selenate caused derepression at one-tenth the concentration of sulfate, a concentration of selenate that was subtoxic, while toxic levels of selenate produced far less derepression. The susceptibility of the tobacco cells to selenate toxicity was high under conditions of sulfur nutrition that derepress ATP sulfurylase, and low under conditions that repress ATP sulfurylase, in agreement with the idea that selenate acts via a functional sulfate assimilation pathway. Since it is known that selenate is incorporated into analogs of sulfur compounds, it is proposed that the tobacco cells synthesize the seleno-analog of the end product of the sulfate pathway responsible for repression, and the seleno-analog antagonizes the normal end product in the repression mechanism, the net result being derepression of ATP sulfurylase by selenate.
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PMID:Derepression of ATP sulfurylase by the sulfate analogs molybdate and selenate in cultured tobacco cells. 26 28

The stability of tryptophan biosynthetic enzyme activities was examined in cultures of repressor-negative (trpR) strains of Escherichia coli K-12 incubated under conditions of nutrient starvation of chloramphenicol inhibition. The results show that four of the five activities examined are stable under most nongrowing conditions, whereas one activity, indoleglycerol phosphate (InGP) synthetase, carried by the trpC protein, is unstable under most conditions tested. Phosphoribosylanthranilate (PRA) isomerase activity, which is also carried by the trpC protein, is unstable during starvation for ammonium, cysteine, or sulfate but is stable under other nongrowing conditions where InGP synthetase is not. InGP synthetase activity but not PRA isomerase activity is also diminished about twofold in cultures using glycerol as a carbon-energy source. These results indicate that one or both activities of the trpC protein is specifically inactivated under several culture conditions. Experiments with antibodies to the trpC protein show that sulfate-starved and ammonium-starved cultures contain 20 to 40% less immunologically reactive trpC protein than unstarved cultures. This indicates that the trpC protein is probably partially degraded under these conditions. During recovery from sulfate starvation or ammonium starvation, cultures slowly regain normal levels of InGP synthetase and PRA isomerase activities, suggesting that inactivation may be reversible.
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PMID:Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli. 32 57

The regulation of uracil uptake in bacteria was studied in bacteriophage T4-infected cells, where host-specific, stable RNA synthesis is completely shut-off by phage, and where phage-specific RNA synthesis, which is not stringently regulated, could be followed by a continuous incorporation of uracil. This incorporation into phage RNA was found to be dependent on the allelic state of the rel gene and it was thus severely restricted under stringent conditions. This was not the case with adenine, which was incorported into RNA to almost the same extent under stringent and relaxed conditions, respectively. The inhibition of uracil uptake under proceeding RNA formation, which was furthermore found to be reversed by addition of chloramphenicol, indicated a specific mechanism governing the cellular entry of uracil. This is suggested to involve the allosteric regulation of uracil phosphoribosyltransferase (EC 2.4.2.9.). The enzyme was partially purified by ammonium sulfate precipitation and gel chromatography. The dependence on GDP and GTP as positive effectors was demonstrated. The stimulatory effect of GTP was abolished in vitro by the addition of guanosine 5'-diphosphate 3-diphosphate, which is known to accumulate during amino acid starvation in stringent bacteria. The reversible inactivation of the enzyme by dilution suggested a subunit structure of uracil phosphoribosyltransferase.
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PMID:Biochemical mechanism of uracil uptake regulation in Escherichia coli B. Allosteric effects on uracil phosphoribosyltransferase under stringent conditions. 33 63

Saccharomyces cerevisiae X2180-1A synthesizes two forms of asparaginase: L-asparaginase I, an internal constitutive enzyme, and asparaginase II, an external enzyme which is secreted in response to nitrogen starvation. The two enzymes are biochemically and genetically distinct. The structural gene for asparaginase I (asp 1) is closely linked to the trp 4 gene on chromosome IV. The gene controlling the synthesis of asparaginase II is not linked to either the trp 4 or asp 1 genes. The rate of biosynthesis of asparaginase II is unaltered in yeast strains carrying the structural gene mutation for asparaginase I. Asparaginase II has been purified approximately 300-fold from crude extracts of Saccharomyces by heat and pH treatment, ethanol fractionation, ammonium sulfate fractionation followed by Sephadex G-25 chromatography, and DEAE-cellulose chromatography. Multiple activity peaks were obtained which, upon gas chromatographic analysis, exhibit varying mannose to protein ratios. Asparaginase I has been purified approximately 100-fold from crude extracts of Saccharomyces by protamine sulfate treatment, ammonium sulfate fractionation, gel permeation chromatography, and DEAE-cellulose chromatography. No carbohydrate component was observed upon gas chromatographic analysis. Comparative kinetic and analytic studies show the two enzymes have little in common except their ability to hydrolyze L-asparagine to L-aspartic acid and ammonia.
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PMID:Characterization of two forms of asparaginase in Saccharomyces cerevisiae. 34 21

A study was made on whether or not the lability of protein generally correlates with its metabolic turnover rate. Two fractions of soluble protein were prepared from rat liver. Using the double isotope method, it was revealed that fraction precipitated with half-saturated ammonium sulfate had a larger turnover rate than the supernatant one. Both dietary protein depletion and starvation, though they significantly decreased total protein content, did not affect the ratio of the amount of protein in the precipitate to that of the supernatant fraction. These results suggested that both fractions, though they had a different turnover rates, were equally influenced by dietary protein depletion or fasting. In consequence, the results imply that the lability of protein does not necessarily in parallel with the metabolic turnover rate.
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PMID:Correlation between lability and relative turnover rate of soluble protein of the rat liver. 60 33

The proteins synthesized by arginine-requiring Escherichia coli during growth or arginine starvation were characterized by polyacrylamide gel electrophoresis in sodium dodecyl sulfate to give size distributions. The proteins made during amino acid starvation were smaller than those made by growing cells. This was true for otherwise isogenic rel- ("relaxed") and rel+ ("stringent") bacteria. Also using electrophoretic profiles, the peptide chain growth rate was estimated by a novel method based on comparison of theoretically predicted and observed kinetics of pulse labeling protein chains of different sizes. During arginine starvation, the rate was 2--5 amino acids/s for both rel- and rel+ cells, compared to 20 amino acids/s for growing cells. The results rule out chain growth-rate differences as an aspect of the "relaxed" phenomenon.
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PMID:The polypeptide chain growth rate in amino acid-starved Escherichia coli determined by a novel method. 76 70


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