Die fetale Indikation f�r die Schnittentbindung

Vara, P

doi:10.1007/bf00674190

Cited by 5 publications

(4 citation statements)

References 7 publications

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“…Proton efflux from the cells was measured after starvation at 4°C and glucose addition at 30°C as described (Serrano, 1980). The formation of the phosphorylated intermediate was as in Vara and Serrano (1983) and the electrophoresis of phosphoenzyme as in Niggli et al (1979). Protein concentration was measured by the method of Bradford (1976), using the Bio-Rad protein assay reagent and bovine globulin as standard.…”

Section: Discussionmentioning

confidence: 99%

Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis.

Portillo¹,

Serrano²

1988

The EMBO Journal

111

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Section: Discussionmentioning

confidence: 99%

Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis.

Portillo¹,

Serrano²

1988

The EMBO Journal

111

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“…Cultures expressing active Kl Pase reach an absorbance of about 1.5 while cultures expressing inactive phenotypes only reach about 0. 3 19,131. The growth medium containcd 2% glucose, 0.7% yeast nitrogen base without amino acids (Difco), 0.2 mM adenine, 0.4 mM histidine and either SO mM succinic acid (taken to pH 4.0 with Tris) or 50 mM Mes (adjusted to pH 6.0 with Tris).…”

mentioning

confidence: 99%

Growth control strength and active site of yeast plasma membrane ATPase studied by site‐directed mutagenesis

Portillo

Serrano

1989

European Journal of Biochemistry

106

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Several amino acids which are conserved in cation-pumping ATPases with phosphorylated intermediate have been mutagenized in the yeast plasma membrane H +-ATPase. The mutant genes have been selectively expressed in a yeast strain where the wild-type ATPase is only expressed in galactose nicdium. A scrics of mutants with decreasing levels of activity demonstrates that the ATPase is rate-limiting for growth and that decreased ATPase activity correlates with decreased intracellular pH. Enzymatic and transport studies of mutant ATPases indicate that (a) Lys474 is the target for the inhibitor fluorescein 5'-isothiocyanate and this residue can be replaced by either arginine or histidine with partial retention of activity; (b) the sensitivity to inhibition by vanadate is affected by the mutations Thr231 --f Gly, Cys376 --f Leu, Lys379 -+ Gin and Asp634 + Asn; (c) the mutation Ser234 + Ala causes uncoupling between ATP hydrolysis and proton transport and reduces the ATP content of the cells; (d) the mutation Asp730 --f Asn, which affects a polar residuc conserved in hydrophobic stretches of H ' -ATPases, abolishes ATPase activity and proton transport but not the formation of a phosphorylated intermediate.The yeast plasma membrane H+-ATPase belongs to a family of cation pumps characterized by the formation of a phosphorylated intermediate. This family, referred to here as (E-P)ATPases, includes bacterial K +

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“…This result argues against the obligatory intermediacy of a proton or sodium gradient in this process. Diethylstilbestrol (DES) is an inhibitor of several plant and fungal ATPases [18,19]. As shown in fig.3, 117/~M DES effectively inhibits ATP synthesis induced by valinomycin addition (at t = 10 min) in M. voltae, which has been shown to result in the formation of a membrane potential, negative inside [9].…”

Section: Resultsmentioning

confidence: 99%

Discrimination between transmembrane ion gradient‐driven and electron transfer‐driven ATP synthesis in the methanogenic bacteria

Al-Mahrouq¹,

Carper²,

Lancaster³

1986

FEBS Letters

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As with Methanococcus voltae [(1986) FEBS Lett. 200, 177-180], ATP synthesis in Methanobacterium thermoautotrophicum (AH) can be driven by the imposition of a sodium gradient, but only in the presence of a counterion. Monensin (but not SF6847) inhibits this synthesis. Methanogenic electron transfer-driven ATP synthesis, however, is insensitive to the combination of these two ionophores. In M. voltae, 117 I~M diethylstilbestrol effectively inhibits both membrane potential-and sodium gradient-driven ATP synthesis, but has no effect on ATP production coupled to methanogenesis. In Mb, thermoautotrophicurn (AII), a similar pattern of inhibition is exhibited by harmaline, an inhibitor of sodium-linked membrane transport systems. We conclude that ATP-driven sodium translocation and electron transfer-driven ATP synthesis are accomplished by separate entities, at least for these two only distantly related species ot methanogen. MethanogenBioenergetics Na + pump A TPase

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Die fetale Indikation f�r die Schnittentbindung

Cited by 5 publications

References 7 publications

Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis.

Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis.

Growth control strength and active site of yeast plasma membrane ATPase studied by site‐directed mutagenesis

Discrimination between transmembrane ion gradient‐driven and electron transfer‐driven ATP synthesis in the methanogenic bacteria

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