SENESCENCE AND THE REGULATION OF CATALASE ACTIVITY AND THE EFFECT OF HYDROGEN PEROXIDE ON NUCLEIC ACIDS**Research supported, in part, by a grant-in-aid from the W. Alton Jones Foundation.

The sensitivity of the formation of plasmonic silver nanoprisms to hydrogen peroxide is explored for the colorimetric detection of catalase activity in bacteria.

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Spectrophotometric determination of hydrogen peroxide: catalase activity and rates of hydrogen peroxide removal by erythrocytes

Clinica Chimica Acta ◽

10.1016/0009-8981(96)06374-7 ◽

1996 ◽

Vol 254 (2) ◽

pp. 101-112 ◽

Cited By ~ 37

Author(s):

Noriyoshi Masuoka ◽

Masahiro Wakimoto ◽

Toshihiko Ubuka ◽

Taku Nakano

Keyword(s):

Hydrogen Peroxide ◽

Spectrophotometric Determination ◽

Catalase Activity ◽

Peroxide Removal

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The formation of choleglobin and the role of catalase in the erythrocyte

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1949.0035 ◽

1949 ◽

Vol 136 (884) ◽

pp. 435-448 ◽

Cited By ~ 11

Keyword(s):

Hydrogen Peroxide ◽

Ascorbic Acid ◽

Amino Acid ◽

Catalase Activity ◽

Acid Oxidase ◽

Small Decrease ◽

Amino Acid Oxidase ◽

Oxidase System ◽

Inverse Proportion

In haemolysates of non-nucleated erythrocytes there is an inverse proportion between catalase activity and rate of choleglobin formation on addition of ascorbic acid. In the intact erythrocytes catalase protects haemoglobin against oxidation and further destruction by the hydrogen peroxide generated by the D-amino-acid oxidase system or by physiological concentrations of ascorbic acid and glutathione. Acid destromatization of haemolyzed horse erythrocytes causes a small decrease in the catalase activity and an increased rate of inactivation of the remaining catalase by ascorbic acid. The liberation of copper from haemocuprein is quantitatively insufficient to explain the decreased stability of the catalase. Exposing duck oxyhaemoglobin, but not reduced haemoglobin, to a pH of 5⋅5 to 5⋅8, causes an alteration which is apparent from the increase of the rate of choleglobin formation. The mechanism of this alteration is discussed. It partly explains the 'stroma effect', at least in duck erythrocytes. In addition, in the latter, there is a true stroma effect. Choleglobin formation in the presence of ascorbic acid is accelerated by a variety of substances. Some of these perturb haemoglobin, while others increase the formation of hydrogen peroxide from ascorbic acid. The implications of our findings on the mechanism of choleglobin formation and on the role of catalase in the erythrocyte are discussed.

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Hydrogen peroxide-inactivated bacteria induces potent humoral and cellular immune responses and releases nucleic acids

International Immunopharmacology ◽

10.1016/j.intimp.2019.01.055 ◽

2019 ◽

Vol 69 ◽

pp. 389-397 ◽

Cited By ~ 4

Author(s):

Yingzi Fan ◽

Yandong Mu ◽

Lian Lu ◽

Yaomei Tian ◽

Fengjiao Yuan ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Immune Responses ◽

Nucleic Acids ◽

Cellular Immune Responses ◽

Cellular Immune

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In Vivo Fitness Adaptations of Colistin-Resistant Acinetobacter baumannii Isolates to Oxidative Stress

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.00598-16 ◽

2016 ◽

Vol 61 (3) ◽

Cited By ~ 8

Author(s):

Crystal L. Jones ◽

Shweta S. Singh ◽

Yonas Alamneh ◽

Leila G. Casella ◽

Robert K. Ernst ◽

...

Keyword(s):

Oxidative Stress ◽

Hydrogen Peroxide ◽

Acinetobacter Baumannii ◽

Catalase Activity ◽

Content Type ◽

Increased Susceptibility

ABSTRACT The loss of fitness in colistin-resistant (CR) Acinetobacter baumannii was investigated using longitudinal isolates from the same patient. Early CR isolates were outcompeted by late CR isolates for growth in broth and survival in the lungs of mice. Fitness loss was associated with an increased susceptibility to oxidative stress since early CR strains had reduced in vitro survival in the presence of hydrogen peroxide and decreased catalase activity compared to that of late CR and colistin-susceptible (CS) strains.

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