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Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Regioselectivity of Electrophilic Additions-Peroxide Effect02:35

Regioselectivity of Electrophilic Additions-Peroxide Effect

In the presence of organic peroxides, the addition of hydrogen bromide to an alkene yields the isomer that is not predicted by Markovnikov’s rule. For example, the addition of hydrogen bromide to 2-methylpropene in the presence of peroxides gives 1-bromo-2-methylpropane. This addition reaction proceeds via a free radical mechanism, which reverses the regioselectivity. The free radical reaction mechanism involves three stages: initiation, propagation, and termination.
Oxidation of Alcohols02:37

Oxidation of Alcohols

In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
Peroxisomes01:24

Peroxisomes

Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...

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Related Experiment Video

Updated: Jul 9, 2026

Quantification of Neurovascular Protection Following Repetitive Hypoxic Preconditioning and Transient Middle Cerebral Artery Occlusion in Mice
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Quantification of Neurovascular Protection Following Repetitive Hypoxic Preconditioning and Transient Middle Cerebral Artery Occlusion in Mice

Published on: May 4, 2015

[Enzymatic mechanisms of inhibition of peroxidative oxidation in different regions of rat brain].

A M Gerasimov, L A Koroleva, O S Brusov

    Voprosy Meditsinskoi Khimii
    |January 1, 1976
    PubMed
    Summary

    This study investigated antioxidant enzyme activity in rat brain regions. The brain stem showed high catalase and superoxide dismutase, while the cerebellum had the most glutathione peroxidase.

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    Cerebral Ischemic Coma Model Induced by Modified Four-Vessel Occlusion

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    Area of Science:

    • Neuroscience
    • Biochemistry
    • Enzymology

    Background:

    • Free-radical processes and oxidative stress are implicated in brain function and disease.
    • Antioxidant enzymes play a crucial role in mitigating oxidative damage in neural tissues.
    • Understanding the regional distribution of these enzymes is vital for comprehending brain's defense mechanisms.

    Purpose of the Study:

    • To quantify the activity of key antioxidant enzymes in different rat brain regions: cortex, cerebellum, and brain stem.
    • To identify the regional distribution patterns of catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and glutathione: dehydroascorbate reductase (GSH:DHR).
    • To investigate the association of thiol-containing substances with proteins in the brain.

    Main Methods:

    • Enzyme activity assays were performed on homogenates from rat brain cortex, cerebellum, and stem.
    • Specific spectrophotometric methods were used to measure the activities of CAT, SOD, GPx, and GSH:DHR.
    • Protein-bound thiol content was analyzed using biochemical techniques.

    Main Results:

    • Enzyme activity varied significantly across brain regions.
    • The brain stem exhibited the highest levels of CAT and SOD.
    • The cerebellum showed the highest GPx activity, while the brain stem had the lowest GPx and GSH:DHR levels.
    • A substantial portion (30-40%) of thiol-containing substances were found to be bound to proteins as mixed disulfides.

    Conclusions:

    • The distinct regional distribution of antioxidant enzymes suggests specialized roles in protecting different brain areas from oxidative stress.
    • The brain stem's high CAT and SOD activity may reflect its higher susceptibility to oxidative damage.
    • GPx levels in the cerebellum indicate its importance in peroxide detoxification in this region.
    • The significant protein-bound thiols suggest their involvement in redox regulation and antioxidant defense within the brain.