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  • 1
    Electronic Resource
    Electronic Resource
    Arsenic mononucleotides. Separation by high-performance liquid chromatography and identification with myokinase and adenylate deaminase (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 955-960 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00300a024
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  • 2
    Electronic Resource
    Electronic Resource
    Catabolite inactivation of the maltose transporter in nitrogen-starved yeast could be due to the stimulation of general protein turnover (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 166 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Addition of glucose to Saccharomyces cerevisiae inactivates the maltose transporter. The general consensus is that this inactivation, called catabolite inactivation, is one of the control mechanisms developed by this organism to use glucose preferentially whenever it is available. Using nitrogen-starved cells (resting cells), it has been shown that glucose triggers endocytosis and degradation of the transporter in the vacuole. We now show that maltose itself triggers inactivation and degradation of its own transporter as efficiently as glucose. This fact, and the observation that glucose inactivates a variety of plasma membrane proteins including glucose transporters themselves, suggests that catabolite inactivation of the maltose transporter in nitrogen-starved cells is not a control mechanism specifically directed to ensure a preferential use of glucose. It is proposed that, in this metabolic condition, inactivation of the maltose transporter might be due to the stimulation of the general protein turnover that follows nitrogen starvation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13907.x
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  • 3
    Electronic Resource
    Electronic Resource
    Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4 (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 147 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The maltose transporter in Saccharomyces cerevisiae is degraded in the vacuole after internalization by endocytosis when protein synthesis is impaired and a fermentable substrate is present. The possible implication of the ubiquitin pathway in this inactivation, known as catabolite inactivation, has been investigated. Using mutants deficient in npi1/rsp5 ubiquitin-protein ligase and npi2/doa4 ubiquitin-protein hydrolase, we have shown that these two enzymes are required for normal endocytosis and degradation of the transporter. These facts indicate that the ubiquitin pathway is involved in catabolite inactivation of the maltose transporter. The results also revealed that both enzymes act in the internalization step of endocytosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10253.x
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  • 4
    Electronic Resource
    Electronic Resource
    Inactivation of the glucose transport system in sporulating yeast (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 41 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The glucose transport system of Saccharomyces cerevisiae was inactivated during sporulation. The glucose uptake capacity of a culture (measured with xylose as substrate) decreased to 50% when about 15% of the population was transformed into asci. At the end of sporulation the residual transport capacity was about 20% of the initial one. No changes in glucose transport were observed in a non-sporulating diploid treated in the same conditions. Reappearance of the transport did not occur during germination if this was inhibited by cycloheximide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02141.x
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  • 5
    Electronic Resource
    Electronic Resource
    Involvement of endocytosis in catabolite inactivation of the K+ and glucose transport systems in Saccharomyces cerevisiae (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 121 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The possible relationship between endocytosis and catabolite inactivation of plasma membrane proteins in Saccharomyces cerevisiae has been investigated. Using mutants with an increased rate of endocytosis we have shown that there is a positive correlation between the rate of endocytosis and the rate of inactivation of the K+ and glucose transport systems. It is concluded that endocytosis is involved in catabolite inactivation of these two transport systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07078.x
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  • 6
    Electronic Resource
    Electronic Resource
    Sugar transport in Saccharomyces cerevisiae (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 104 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The yeast Saccharomyces cerevisiae consumes mono- and disaccharides preferentially to any other carbon source. Since sugars do not freely permeate biological membranes, cellular uptake of these compounds requires the action of ‘transporters’. The purpose of this review is to summarize the present knowledge on sugar transport in this organism. Yeast cells show two transporters for monosaccharides, the so-called glucose and galactose transporters that act by a facilitated diffusion mechanism. In the case of glucose transport, which also acts upon d-fructose and d-mannose, two components with high- and low-affinity constants have been identified kinetically. Activity of the high-affinity component is dependent on the presence of active kinases whereas activity of the low-affinity component is independent of the presence of these enzymes. Three genes, SNF3, HXT1 and HXT2, encode three different glucose transporters with a high affinity for the substrates and are repressed by high concentrations of glucose in the medium. Kinetic studies suggest that at least one additional gene exists that encodes a transporter with a low affinity and is expressed constituently. The present view is that there are several additional transporters for glucose that have not yet been identified. Galactose transport has only one natural substrate, d-galactose, and is encoded by the gene GAL2. Expression of this gene is induced by galactose and repressed by glucose. Two transporters for disaccharides have been identified in S. cerevisiae: maltose and α-methylglucoside transporters. These transporters are H+-symports that depend on the electrochemical proton gradient and are independent of the ATP level. The gene that encodes the maltose transporter is clustered with the other two genes required for maltose utilization in a locus that is found repeated at different chromosomal locations. Its expression is induced by maltose and repressed by glucose. The rate of sugar uptake in yeast cells is controlled by changes in affinity of the corresponding transporters as well as by an irreversible inactivation that affects their Vmax. The mechanisms involved in these regulatory processes are unknown at present.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb05869.x
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  • 7
    Electronic Resource
    Electronic Resource
    The calculation of cellular parameters from the turbidity of yeast cultures may give rise to important errors (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 29 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract It is shown that cellular parameters of the yeast cultures (e.g. intracellular volume, cellular dry weight, protein content, number of cells, and turbidity) are differently influenced by metabolic changes. Therefore, the cellular parameters change independently of each other. It is hence concluded that whenever quantitation is required, the values of these parameters should be measured independently and not calculated from the turbidity of the cultures or other parameters, as is often done.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00886.x
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  • 8
    Electronic Resource
    Electronic Resource
    Orthophosphate determination: A simple spectrophotometric method for the measurement of the orthophosphate-triethylamine-molybdate complex (1979)
    Springer
    Microchimica acta 72 (1979), S. 181-185 
    Details
    ISSN: 1436-5073
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Triäthylamin ist ein selektives Fällungsreagens für Phosphormolybdänsäure, das die Trennung von Orthophosphat aus Mischungen von Phosphorsäureestern und Anhydriden erlaubt. Eine einfache Methode zur Bestimmung von Orthophosphat-Triäthylamin-Molybdat wurde beschrieben. Sie beruht auf der Messung der Ultraviolett-Absorption des Komplexes. Fünf bis 250 nMol gefälltes Orthophosphat werden in 3 ml Methanol gelöst und die Absorption dieser Lösung gegen Wasser bei 320 nm gemessen. Der molare Extinktionskoeffizient des Komplexes unter diesen Bedingungen ist 2,09·107 1·Mol−1·cm−1.
    Notes: Summary Triethylamine is a selective precipitant for phosphomolybdic acid which allows separation of orthophosphate from phosphoric acid esters and anhydrides. In this paper a simple method for the estimation of the orthophosphate-triethylamine-rnolybdate complex, based on its ultraviolet absorption spectrum, is described. The precipitate, corresponding to a range of 5–250 nmole of orthophosphate, is dissolved in 3 ml of methanol and the absorbance of the solution measured at 320 nm against water. The molar absorptivity of the complex at this wavelength is 2.09 × 1071·mole−1·cm−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01197370
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  • 9
    Electronic Resource
    Electronic Resource
    Determination of intermediary metabolites in yeast. Critical examination of the effect of sampling conditions and recommendations for obtaining true levels (1976)
    Springer
    Molecular and cellular biochemistry 13 (1976), S. 73-78 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The effect of sampling conditions on the levels of adenine nucleotides, pyridine nucleotides, glycolytic intermediates and related metabolites in yeast has been studied. A systematic examination of the conditions for harvesting has shown that it can be best accomplished by rapid filtration. Delays in the handling for removal of the medium, as is usual in the process of obtaining a number of data reported in the literature, lead to important changes in some of the metabolites examined. It is also shown that when a washing is imperative it can be carried out with a methanol-water mixture (50/50, v/v) cooled at −40° without loss of intracellular concentrations of non-readily diffusible metabolites. On the basis of this experience the outline of a generally applicable procedure is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01837056
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  • 10
    Electronic Resource
    Electronic Resource
    Effectors of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver. (1977)
    Springer
    Molecular and cellular biochemistry 17 (1977), S. 147-149 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The lower Vmax of 6PGDH with respect to G6PDH and its higher sensitivity to inhibition by NADPH, suggest the existence of an imbalance between the two dehydrogenases of the pentose phosphate pathway in rat liver. Possible modulators of these activities, particularly in relation with the inhibition by NADPH in physiological conditions, have been investigated. The results suggest that in both cases the inhibition by NADPH is strictly isosteric and that the relative affinities for the reduced and oxidized forms of the pyridine nucleotide are unaffected by glutathion, the intermediates of the pentose phosphate shunt or some divalent ions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01730834
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