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Related Concept Videos

Peroxisomes01:24

Peroxisomes

13.6K
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...
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Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

4.6K
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...
4.6K
Radical Autoxidation01:20

Radical Autoxidation

2.5K
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...
2.5K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

4.4K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
4.4K
Autoxidation of Ethers to Peroxides and Hydroperoxides02:23

Autoxidation of Ethers to Peroxides and Hydroperoxides

8.2K
Ethers represent a class of chemical compounds that become more dangerous with prolonged storage because they tend to form explosive peroxides when standing in the air. Autoxidation is the spontaneous oxidation of a compound in air. In the presence of oxygen, ethers slowly oxidize to form hydroperoxides and dialkyl peroxides.
8.2K
Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide02:44

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

11.1K
Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.
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Peroxidase activity in Linum usitatissimum L.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2014
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Cytoplasmic effects on peroxidase activity in crosses between two genotypes of flax (Linum usitatissimum L.).

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·2014

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Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
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Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

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Peroxidase isoenzymes in Linum.

H Tyson1, R Bloomberg

  • 1Genetics Department, McGill University, Montreal, Canada.

TAG. Theoretical and Applied Genetics. Theoretische Und Angewandte Genetik
|January 17, 2014
PubMed
Summary

Peroxidase isoenzyme activity in flax (Linum usitatissimum L.) was analyzed across generations. Both genetic and maternal factors influenced isoenzyme expression, correlating with overall enzyme activity.

Area of Science:

  • Plant genetics and molecular biology
  • Enzyme kinetics and protein analysis

Background:

  • Peroxidases are crucial enzymes involved in plant defense and development.
  • Understanding isoenzyme expression patterns is key to plant breeding and genetic studies.

Purpose of the Study:

  • To investigate the genetic basis of peroxidase isoenzyme activity in Linum usitatissimum L.
  • To analyze the relationship between gross peroxidase activity and specific isoenzyme profiles.
  • To determine the influence of genetic and maternal effects on isoenzyme expression across generations.

Main Methods:

  • Acrylamide gel electrophoresis was used to separate peroxidase isoenzymes.
  • Enzyme activity was measured in main stem tissue homogenates before and after electrophoresis.
  • Analysis was conducted on two Linum usitatissimum L. genotypes and their F1, F2, and backcross progeny.

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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes

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Last Updated: May 4, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
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Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples

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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes

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Main Results:

  • A strong correlation was observed between gross peroxidase activity and specific isoenzyme activity.
  • Distinct isoenzyme profiles were identified in different genotypes and generations.
  • Evidence indicated both genetic and maternal influences on peroxidase isoenzyme activity.

Conclusions:

  • Peroxidase isoenzyme expression in Linum usitatissimum L. is significantly influenced by genetic and maternal factors.
  • The study provides insights into the inheritance patterns of peroxidase isoenzymes in flax.
  • Findings contribute to understanding enzyme variation and its implications in plant genetics.