The Relationship of Hydrogen Peroxide to the Inhibition of the Glyoxalase Activity of Intact Erythrocytes by X-Radiation

Klebanoff, Seymour J.

doi:10.1085/jgp.41.4.737

Cited by 8 publications

(3 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, the concentration of H202 in the suspension decreases and allows the cells to survive. This problem was eliminated by using an H202-generating system (19). This system ensures a relatively constant concentration of H202 throughout the experiment.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus

Sammartano¹,

Tuveson²,

Davenport³

1986

J Bacteriol

View full text Add to dashboard Cite

Mutations in the Escherichia coli katF gene (hydroperoxidase II) result in sensitivity to inactivation by H202 and broad-spectrum near-UV (NUV; 300 to 400 nm) radiation. Another mutation, nur, originally described as conferring sensitivity to inactivation by broad-spectrum and monochromatic NUV, also confers sensitivity to inactivation by H202. Genetic analysis via transduction suggests that the nur mutation is a mutant allele of the katF locus. As previously reported for broad-spectrum and monochromatic NUV wavelengths, the sensitivity of a particular strain to H202 inactivation is also independent of the recA and uvrA alleles. Extracts of nur and katF strains lack catalase (hydroperoxidase II) as revealed by polyacrylamide gels stained for such activity, which is consistent with the genetic results.The mutagenic and inactivating effects of both monochromatic and broad-spectrum near-UV (NUV) wavelengths (300 to 400 nm) have been the subject of numerous investigations, which have been extensively reviewed (10,13,17,18,40).A mutation in an Escherichia coli gene (nur) has been described which sensitizes cells to inactivation by NUV without affecting sensitivity to far-UV (FUV) inactivation (35-37). Specifically, it was shown that the recA13, recAl, and uvrA6 mutations did not affect the sensitivity of stationary-phase cells to NUV inactivation. However, the polAl mutation did influence the sensitivity of E. coli cells to inactivation by NUV in an nur+ genetic background (36). The fact that the polAl mutation sensitizes E. coli to NUV inactivation and that E. coli xthA mutants (exonuclease III deficient) are sensitive to inactivation by H202 (8) and NUV (31) might mean that repair of or protection against NUVand H202-induced damage is based on a complex oxidative defense system (4).Further evidence that H202 is involved in NUV inactivation comes from the observation that incorporation of bovine catalase into the plating medium or the irradiated cell suspension protects E. coli cells from both inactivation and mutagenesis by broad-spectrum NUV (32). Hartman (14) has also presented evidence that H202 is involved with NUV inactivating events in stationary-phase E. coli cells.Pretreatment of E. coli or Salmonella typhimurium cells with a sublethal concentration of H202 results in protection against inactivation by a lethal concentration of H202 (4, 7) as well as by broad-spectrum NUV (33, 39). Tyrrell (39) has shown that pretreatment of growing E. coli cells with low fluences of NUV protects against inactivation by H202. If H202 were one product of NUV irradiation in cells, it would be expected that cells lacking catalase should be sensitive to inactivation by NUV. Recently, Leowen and his colleagues have described mutants which are defective in catalase activity (21)(22)(23). In this paper, we present evidence that lesions in the katF gene, but not the katE or katG gene, result in sensitivity to broad-spectrum NUV as well as to * Corresponding author.

show abstract

Section: Discussionmentioning

confidence: 99%

“…Therefore, strains RT7h (nur) and RT9h (nur+) were suspended in an enzyme reaction mixture designed to generate 1 mM of H202 per min as a product of the glucose oxidase reaction (glucose + 02 -> gluconic acid + H202 [19]). The results of these experiments are presented in Fig.…”

mentioning

confidence: 99%

Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus

Sammartano¹,

Tuveson²,

Davenport³

1986

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…However, it was considered that reduced glutathione of human erythrocytes might cause uncontrolled reactivation of PCMB-treated virus at 37°C. Such reactivation would not be expected to occur if hydrogen peroxide-treated erythrocytes were used, because hydrogen peroxide oxidizes the reduced glutathione in erythrocytes (18).…”

Section: Eject Of Pcmb On Adsorption Of Virus To Erythrocytes--inactmentioning

confidence: 99%

On the Role of Virus Sulfhydryl Groups in the Attachment of Enteroviruses to Erythrocytes

Philipson¹,

Choppin²

1960

The Journal of Experimental Medicine

View full text Add to dashboard Cite

Many animal viruses possess the ability to agglutinate erythrocytes. In most but not all cases hemagglutination is due to the virus particle itself, and appears to result from the mechanical bridging of two or more erythrocytes by virus particles which attach to receptor sites on each erythrocyte (1, 2). Thus, attachment of virus particles to erythrocytes is a prerequisite for hemagglutination, and prevention of absorption of virus prevents hemagglutination. Among the enteroviruses, many ECHO viruses and some strains of Coxsackie B3 virus agglutinate human erythrocytes (3-7), and the evidence indicates that hemagglutination is due to the virus particle itself (3, 5, 6). The precise mechanism of attachment of enteroviruses to cells is unknown. Chymotrypsin treatment of erythrocytes prevents the absorption of some ECHO viruses (8). This suggests that the receptor sites on the erythrocyte may be at least in part protein in nature. The present communication is concerned with the mechanism of attachment of enteroviruses to cells. It is shown that sulfhydryl reagents block the hemagglutinating activity of enteroviruses. Treated virus fails to absorb to erythrocytes. Thiol compounds restore the hemagglutinating activity of enteroviruses treated with mercaptide-forming sulfhydryl reagents. The effect of sulfhydryl reagents on the infectivity of some enteroviruses is also described.

show abstract

Die Veränderungen der Michaelis-Konstanten des Pepsins und Trypsins mit verschiedenen bestrahlten Proteinen und die chromatographische und elektrophoretische Trennung der proteolytisch entstandenen Spaltprodukte

Prellwitz

1965

Klin Wochenschr

View full text Add to dashboard Cite

The Relationship of Hydrogen Peroxide to the Inhibition of the Glyoxalase Activity of Intact Erythrocytes by X-Radiation

Cited by 8 publications

References 18 publications

Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus

Control of sensitivity to inactivation by H2O2 and broad-spectrum near-UV radiation by the Escherichia coli katF locus

On the Role of Virus Sulfhydryl Groups in the Attachment of Enteroviruses to Erythrocytes

Die Veränderungen der Michaelis-Konstanten des Pepsins und Trypsins mit verschiedenen bestrahlten Proteinen und die chromatographische und elektrophoretische Trennung der proteolytisch entstandenen Spaltprodukte

Contact Info

Product

Resources

About