Application of an integrated rate equation to the inactivation of catalase

Feuers, Ritchie J.; Pattillo, Francis M.; Osborn, Criston K.; Adams, Karen; DeLuca, Donald C.; Smith, W. L.

doi:10.1016/0891-5849(93)90063-z

Cited by 13 publications

(21 citation statements)

References 11 publications

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“…Inactivation and reactivation of catalase in vivo and in vitro are far from being fully understood. Numerous recent publications suggest new approaches regarding in vitro assays and inhibition studies on catalase (Feuers et al, 1993;DeLuca et al, 1995;Wolff, 1994, 1996;Escobar et al, 1996;Hook and Harding, 1996). In the present report, we provide new insights into SA's effects on catalase.…”

mentioning

confidence: 68%

“…There is increasing interest in the involvement of oxidative stress in environmental pollution, aging, diabetes, cancer, and other human diseases and in catalase's role as one of the main antioxidative enzymes. In particular, this has led to renewed interest in the mechanism of catalase inhibition and inactivation (Feuers et al (1993), Hillar et al (1994), DeLuca et al (1995), Wolff (1994, 1996), Escobar et al (1996), and references therein).…”

Section: Discussionmentioning

confidence: 99%

“…Although an initial H 2 O 2 concentration of 10 mM may seem high, it was used routinely by Chance and others (reviewed by Schonbaum and Chance (1976)) to study inactivation of catalase in vitro. Under these conditions, high H 2 O 2 levels are maintained for only short periods after the addition of catalase; however, this method is commonly used to assay the susceptibility of catalase to H 2 O 2 (Feuers et al, 1993;DeLuca et al, 1995). It is well established that catalase is inactivated by its own substrate, H 2 O 2 (Kirkman et al, 1987;DeLuca et al, 1995).…”

Section: Fig 1 Separation Of Tobacco Leaf Catalase Isoforms By Chromentioning

confidence: 99%

“…There is increasing evidence that catalase is a major factor in a variety of pathological states such as cancer, diabetes, aging, and oxidative stress (see DeLuca et al (1995); Feuers et al (1993)). Inactivation and reactivation of catalase in vivo and in vitro are far from being fully understood.…”

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confidence: 99%

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Salicylic Acid Is a Modulator of Tobacco and Mammalian Catalases

Durner

Klessig

1996

Journal of Biological Chemistry

296

154

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Salicylic acid (SA) plays a key role in the establishment of resistance to microbial pathogens in many plants. The discovery that SA inhibits catalase from tobacco led us to suggest that H 2 O 2 acts as second messenger to activate plant defenses. Detailed analyses of SA's interaction with tobacco and mammalian catalases indicate that SA acts as an electron donor for the peroxidative cycle of catalase. When H 2 O 2 fluxes were relatively low (1 M/min or less), SA inhibited catalase, consistent with its suggested signaling function via H 2 O 2 . However, significant inhibition was only observed at 100 M SA or more, a level reached in infected, but not in uninfected, leaves. This inhibition was probably due to siphoning catalase into the slow peroxidative reaction. Surprisingly, SA was also able to protect catalase from inactivation by damaging levels of H 2 O 2 (lower millimolar range), which is generally assumed to reflect accumulation of inactive ferro-oxy intermediates. SA did so by supporting or substituting for the protective function of catalase-bound NADPH. These results add new features to SA's interaction with heme enzymes and its in vivo redox properties. Thus, SA, in addition to its proposed signaling function, may also have an important antioxidant role in containing oxidative processes associated with plant defense responses.

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mentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Section: Fig 1 Separation Of Tobacco Leaf Catalase Isoforms By Chromentioning

confidence: 99%

mentioning

confidence: 99%

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Salicylic Acid Is a Modulator of Tobacco and Mammalian Catalases

Durner

Klessig

1996

Journal of Biological Chemistry

296

154

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“…We believe that describing the effective CAT activity by this method takes into account the period of time required for inactivation of the enzyme by H202 (i.e., resistance to substrate inhibition). Additionally, this type approach has been validated as an useful mathematical model for expression of CAT activity (19).…”

Section: Catalase Assaymentioning

confidence: 99%

Increased effective activity of rat liver catalase by dietary restriction

Feuers

Weindruch

Leakey³

et al. 1997

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While dietary restriction (DR) increases maximum life span in many animal species, the mechanisms by which this is achieved remain unclear. One possibility is that DR may act in part to reduce free radical levels by retarding age-related declines in rat liver catalase activity. We measured liver cytosolic catalase activity at various times of day in 9-12 month old male (BN X F344)F1 rats fed ad libitum (AL) or subjected to a 30% DR from 14 weeks of age. Catalase activity (expressed as μmol·min(-1)·g liver(-1)) in both diet groups reached minimums at 0600 h but activity was 26% higher in DR as compared to AL rats. This traditional expression of catalase activity did not significantly differ between diet groups at other times of day. One must be careful in the interpretation of such data, however, since catalase is rapidly inactivated by its substrate (H2O2), thus displaying abnormal enzyme kinetics. In order to avoid this difficulty we evaluated the time period during which the reaction remained linear and multiplied it by its activity to yield the effective catalase activity. Using this method we found a significant increase in catalase activity in DR animals at several H2O2 concentrations during the light span. At 1800 h (the beginning of the dark span when the controls initiated peak food intake), fewer and smaller dietary differences were observed and no dietary effects were observed at 2400 h. These data suggest that DR reduces the rate of accumulation of inactive catalase and may contribute to an increased capacity in DR animals to remove free radicals.

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