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1.
C T Lago G Sannia G Marino C H Squires J M Calvo M De Felice 《Biochimica et biophysica acta》1985,824(1):74-79
The ilvI and ilvH gene products were identified physically by electrophoretic analysis of in vivo-labelled polypeptides produced in minicells from plasmids carrying the wild-type ilvIH operon of Escherichia coli K-12 and derivatives of it. An analysis of the distribution of methionine residues in the amino-terminal portion of micro-quantities of the ilvI product eluted from gel showed that the translational start of the ilvI gene is the promoter-proximal one of three putative methionine codons predicted from the DNA sequence. 相似文献
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Vincenzo Carelli Antonio Casini Alessandro Finazzi-Agro Felice Liberatore Silvano Tortorella 《Free radical research》1988,4(6):397-402
The nicotinamide adenine dinucleotide dimers (NAD)2 obtained by electrochemical reduction of NAD+ are oxidized by adriamycin in anaerobic photocatalyzed reaction yielding NAD+ and 7-deoxyadriamyci-none. Under the same conditions NADH is not oxidized. 相似文献
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Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria 总被引:2,自引:0,他引:2
Ewa Lenartowicz Paolo Bernardi Giovanni Felice Azzone 《Journal of bioenergetics and biomembranes》1991,23(4):679-688
This paper reports an investigation on the effects of the hydrophobic, bifunctional SH group reagent phenylarsine oxide (PhAsO) on mitochondrial membrane permeability. We show that PhAsO is a potent inducer of the mitochondrial permeability transition in a process which is sensitive to both the oxygen radical scavanger BHT and to cyclosporin A. The PhAsO-induced permeability transition is stimulated by Ca2+ but takes place also in the presence of EGTA in a process that maintains its sensitivity to BHT and cyclosporin A. Our findings suggest that, at variance from other known inducers of the permeability transition, PhAsO reacts directly with functional SH groups that are inaccessible to hydrophilic reagents in the absence of Ca2+. 相似文献
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Maurilio De Felice John Guardiola Maria C. Malorni Tadeusz Klopotowski Maurizio Iaccarino 《Journal of bacteriology》1974,120(3):1058-1067
Three mutations (ilvH611, ilvH612, and ilvH613) are described which make Escherichia coli K-12 resistant to valine inhibition and are located near leu. The expression of the ilv genes appears to be normal in these mutants since the isoleucine-valine biosynthetic enzymes are not derepressed relative to the wild type. The intracellular concentration of valine is, however, higher in the mutants than in the isogenic ilvH(+) strain. These mutants also excrete valine, probably because of the high intracellular concentration of this amino acid. The pool size of valine is regulated independently from that of isoleucine and leucine. The increased intracellular concentration of valine is due to a decreased feedback inhibition that valine exerts on its own biosynthetic pathway. In fact, acetolactate synthase activity assayed in extracts of ilvH612 and ilvH613 mutants is more resistant to valine inhibition than the activity assayed in the ilvH(+) isogenic strain. Two forms of acetolactate synthase activity can be separated from these extracts by adsorption and elution on hydroxylapatite. One of them is as sensitive to valine inhibition as that of the wild type, the other is more resistant to valine inhibition. 相似文献
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Structural Genes for a Newly Recognized Acetolactate Synthase in Escherichia coli K-12 总被引:23,自引:15,他引:8 下载免费PDF全文
Maurilio De Felice John Guardiola Bruno Esposito Maurizio Iaccarino 《Journal of bacteriology》1974,120(3):1068-1077
Evidence is reported that shows the presence in Escherichia coli K-12 of a newly found acetolactate synthase. This enzyme is the product of two genes, ilvH and ilvI, both located very close to leu. Amber mutations have been found in both genes and therefore their products are polypeptides. Mutations in the ilvH gene cause the appearance of an acetolactate synthase activity which is relatively resistant to valine inhibition and can be separated by adsorption on hydroxylapatite from another activity present in the extract and more sensitive to valine inhibition than the former. A mutant altered in the ilvI gene was isolated among the revertants sensitive to valine inhibition of an ilvH mutant. Such a mutant lacks the resistant acetolactate synthase. A temperature-sensitive revertant of the ilvI mutant contained a temperature-sensitive acetolactate synthase. Thus ilvI is the structural gene for a specific acetolactate synthase. The activity of the ilvH gene product has been measured by adding an extract containing it to a purified ilvI acetolactate synthase, which, upon incubation, became more sensitive to valine inhibition. Conversely, a valine-sensitive acetolactate synthase (the product of the ilvH and the ilvI genes) became more resistant to valine inhibition upon incubation with an extract of a strain containing a missense ilvH gene product. 相似文献
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