Eosinophil peroxidase is also partly responsible for tissue remodeling.

It is formed by eosinophil peroxidase.

The oxidizing compounds produced by eosinophil peroxidase have been implicated in the inflammatory pathology of several disease states, including asthma.

For example, although eosinophil peroxidase is able to oxidize chloride, it preferentially oxidizes bromide.

Major basic protein, eosinophil peroxidase, and eosinophil cationic protein are toxic to many tissues.

Eosinophil peroxidase is a haloperoxidase enzyme that in humans is encoded by the EPX gene.

For example, eosinophil peroxidase appears to prefer bromide over chloride, yet is not considered a bromoperoxidase because it is able to use chloride.

Eosinophil peroxidase is a haloperoxidase that preferentially uses bromide over chloride for this purpose, generating hypobromite (hypobromous acid).

Eosinophil peroxidase forms reactive oxygen species and reactive nitrogen intermediates that promote oxidative stress in the target, causing cell death by apoptosis and necrosis.

The compound is generated in warm-blooded vertebrate organisms especially by eosinophils, which produce it by the action of eosinophil peroxidase, an enzyme which preferentially uses bromide.

Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase.

The recruited eosinophils will degranulate releasing a number of cytotoxic molecules (including Major Basic Protein and eosinophil peroxidase) as well as produce a number of cytokines such as IL-5.

Heme l is one important characteristic of animal peroxidases; plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus.

The staining is concentrated in small granules within the cellular cytoplasm, which contain many chemical mediators, such as histamines and proteins such as eosinophil peroxidase, ribonuclease (RNase), deoxyribonucleases, lipase, plasminogen, and major basic protein.

In the presence of HO formed by the eosinophil, and either chloride or bromide ions, eosinophil peroxidase provides a potent mechanism by which eosinophils kill multicellular parasites (such as, for example, the nematode worms involved in filariasis); and also certain bacteria (such as tuberculosis bacteria).

Eosinophil peroxidase is also partly responsible for tissue remodeling.

It is formed by eosinophil peroxidase.

The oxidizing compounds produced by eosinophil peroxidase have been implicated in the inflammatory pathology of several disease states, including asthma.

For example, although eosinophil peroxidase is able to oxidize chloride, it preferentially oxidizes bromide.

Major basic protein, eosinophil peroxidase, and eosinophil cationic protein are toxic to many tissues.

Eosinophil peroxidase is a haloperoxidase enzyme that in humans is encoded by the EPX gene.

For example, eosinophil peroxidase appears to prefer bromide over chloride, yet is not considered a bromoperoxidase because it is able to use chloride.

Eosinophil peroxidase is a haloperoxidase that preferentially uses bromide over chloride for this purpose, generating hypobromite (hypobromous acid).

Eosinophil peroxidase forms reactive oxygen species and reactive nitrogen intermediates that promote oxidative stress in the target, causing cell death by apoptosis and necrosis.

The compound is generated in warm-blooded vertebrate organisms especially by eosinophils, which produce it by the action of eosinophil peroxidase, an enzyme which preferentially uses bromide.

Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase.

The recruited eosinophils will degranulate releasing a number of cytotoxic molecules (including Major Basic Protein and eosinophil peroxidase) as well as produce a number of cytokines such as IL-5.

Heme l is one important characteristic of animal peroxidases; plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus.

The staining is concentrated in small granules within the cellular cytoplasm, which contain many chemical mediators, such as histamines and proteins such as eosinophil peroxidase, ribonuclease (RNase), deoxyribonucleases, lipase, plasminogen, and major basic protein.

In the presence of HO formed by the eosinophil, and either chloride or bromide ions, eosinophil peroxidase provides a potent mechanism by which eosinophils kill multicellular parasites (such as, for example, the nematode worms involved in filariasis); and also certain bacteria (such as tuberculosis bacteria).