A product from the iodination of MONOIODOTYROSINE. In the biosynthesis of thyroid hormones, diiodotyrosine residues are coupled with other monoiodotyrosine or diiodotyrosine residues to form T4 or T3 thyroid hormones (THYROXINE and TRIIODOTHYRONINE).
A product from the iodination of tyrosine. In the biosynthesis of thyroid hormones (THYROXINE and TRIIODOTHYRONINE), tyrosine is first iodized to monoiodotyrosine.
An enzyme derived from cow's milk. It catalyzes the radioiodination of tyrosine and its derivatives and of peptides containing tyrosine.
A metabolite of AMINOPYRINE with analgesic and anti-inflammatory properties. It is used as a reagent for biochemical reactions producing peroxides or phenols. Ampyrone stimulates LIVER MICROSOMES and is also used to measure extracellular water.
Inorganic binary compounds of iodine or the I- ion.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
Thyroglobulin is a glycoprotein synthesized and secreted by thyroid follicular cells, serving as a precursor for the production of thyroid hormones T3 and T4, and its measurement in blood serves as a tumor marker for thyroid cancer surveillance.
Enlargement of the THYROID GLAND that may increase from about 20 grams to hundreds of grams in human adults. Goiter is observed in individuals with normal thyroid function (euthyroidism), thyroid deficiency (HYPOTHYROIDISM), or hormone overproduction (HYPERTHYROIDISM). Goiter may be congenital or acquired, sporadic or endemic (GOITER, ENDEMIC).
A highly vascularized endocrine gland consisting of two lobes joined by a thin band of tissue with one lobe on each side of the TRACHEA. It secretes THYROID HORMONES from the follicular cells and CALCITONIN from the parafollicular cells thereby regulating METABOLISM and CALCIUM level in blood, respectively.
Natural hormones secreted by the THYROID GLAND, such as THYROXINE, and their synthetic analogs.

Interaction of diiodo-L-tyrosine and triiodophenol with bovine serum albumin. Circular dichroism and fluorescence studies. (1/25)

As a model study to investigate the binding mechanism between thyroid hormones and carrier protein, the interaction of diiodo-L-tyrosine (DIT) and triiodophenol (I3phi) with bovine serum albumin (BSA) was investigated by circular dichroism (CD) and fluorescence methods. In both the DIT-BSA system and the I3phi-BSA system, induced Cotton effect was observed in the wavelength region near 320 nm. This induced Cotton effect was measured at various molar ratios of ligands to BSA (L/P). The value of the ellipticity at 319 nm, [theta]319, in the I3phi-BSA system was remarkably large compared with that of the DIT-BSA system, and [theta]319 at an L/P ratio of one was -1.96 X 10(4) (degree cm2 decimole-1) for the I3phi-BSA system and -0.1 X 10(4) for the DIT-BSA system. The binding constants for the combination of BSA with a single molecule of ligand, calculated by measuring the quenching of the fluorescence of the protein, were 1.33 X 10(5) M(-1) at 15 degrees for the DIT-BSA system and 1.6 X 10(9) M(-1) at 28 degrees for the I3theta-BSA system. These results suggest that the binding of I3theta to BSA is stronger than that of DIT and a cleft may exist more congruent with the molecular dimensions of I3theta than with those of DIT.  (+info)

A multiple ligand-binding radioimmunoassay of diiodotyrosine. (2/25)

A radioimmunoassay has been developed for the measurement of 3,5-diiodo-L-tyrosine (DIT) in serum. DIT was coupled to porcine thyroglobulin (PTg) with a molar ratio of 205:1. Rabbits were immunized with 1 mg of immunogen emulsified in complete Freund's adjuvant. Sera were screened for their ability to bind trace amounts of [125I]DIT. A serum that bound 40% of the tracer at a final dilution of 1:1,750 was used in the assay. Assay specificity was improved by the use of thyroxine (T4)-binding globulin as a second ligand-binding protein to decrease T4 and triiodothyronine (T3) cross-reactivity with the antibody. Double antibody and polyethylene glycol radioimmunoassays were compared. DIT present in the second antiserum shifted the double antibody assay standard curve and altered estimates of assay specificity and assay sensitivity. By using the polyethylene glycol system and butanol:ethanol extracts of serum, DIT was measured in human serum. In 35 apparently healthy young adult controls DIT levels averaged 156 ng/100 ml. Random DIT levels averaged 158 ng/100 ml in 11 untreated hyperthyroid patients and 84 ng/100 ml in 15 untreated primary hypothyroid patients. No diurnal pattern in DIT levels could be demonstrated. Thyroid-stimulating hormone administration led to a variable but small rise in DIT levels, but short term T3 suppression was not associated with a measurable fall in DIT concentrations. Paired serum samples from the carotid artery and thyroid vein of 10 euthyroid goiter patients and one patient with a toxic solitary adenoma all showed a positive transthyroidal gradient indicating the thyroidal release of DIT in each patient. Measurable DIT levels of 45, 47, 68, and 80 ng/100 ml, respectively, were found in four fasting athyrotic patients indicating that the thyroid is not the only source of serum DIT.  (+info)

Free diiodotyrosine effects on protein iodination and thyroid hormone synthesis catalyzed by thyroid peroxidase. (3/25)

Free diiosotyrosine exerts two opposite effects on the reactions catalyzed by thyroid peroxidase, thyroglobulin iodination and thyroid hormone formation. 1. Inhibition of thyroglobulin iodination catalyzed by thyroid peroxidase was observed when free diiodotyrosine concentration was higher than 5 muM. This inhibition was competitive, suggesting that free diiodotyrosine interacts with the substrate site(s) of thyroid peroxidase. Free diiodotyrosine also competively inhibited iodide peroxidation to I2. 2. Free diiodotyrosine, when incubated with thyroid peroxidase in the absence of iodide was recovered unmodified; in the presence of iodide an exchange reaction was observed between the iodine atoms present in the diiodotyrosine molecule and iodide present in the medium. Using 14C-labelled diiodotyrosine, 14C-labelled non-iodinated products were also observed, showing that deiodination occurred as a minor degradation pathway. However, no monoiodo[14C]tyrosine or E114C]tyrosine were observed. Exchange reaction between free diiototyrosine and iodide is therefore direct and does not imply deiodination-iodination intermediary steps. Thyroglobulin inhibits diiodotyrosine-iodide exchange and vice versa, again suggesting competition for both reactions. These results support, by a different experimental approach, the two-site model for peroxidase previously described by us in this journal. 3. Free diiodotyrosine when present at a very low concentration, 0.05 muM, exerts a stimulatory effect on throid hormones synthesis. The relationship between diiodotyrosine concentration and thyroid hormone synthesis give an S-shaped curve, suggesting that free diiodotyrosine acts as a regulatory ligand for thyroid peroxidase. Evidence is also presented that free diiodotyrosine is not incorporated into thyroid hormones. Therefore, thyroid peroxidase catalyzes only intra-molecular coupling between iodotyrosine hormonogenic residues. 4. Finally, although no direct proof exists that these free diiodotyrosine effects upon thyroglobulin iodination and thyroid hormone synthesis are physiologically significant, such a possibility deserves further investigation.  (+info)

The effect of iodide administration on hog thyroid gland and the composition of thyroglobulin and 27-S iodoprotein. (4/25)

The effect of excess iodide on hog thyroid gland has been examined with regard to the change in the chemical composition of thyroglobulin and in the accumulation of 27-S iodoprotein by the in vivo treatment of hogs with iodide for various lengths of time. The iodine content of thyroglobulin was either unchanged by short term administration of excess iodide, or somewhat lowered. However, the iodine content as well as the total amount of thyroglobulin increased in the glands enlarged by prolonged treatment with iodide. The iodine highest reached 1.17% of the protein on an average. On the other hand, 27-S iodoprotein decreased and finally disappeared after the chronic treatment. Monoiodotyrosine and diiodotyrosine increased in parallel with the increase in the iodine content (0.15 to 1.17%) caused by the iodide treatment, while thyroxine increased but reached a plateau at the level of three residues per mole of thyroglobulin, and no change was observed even in the proteins with the higher iodine content than 0.75%. Proteolytic activity measured by amino acid release from the thyroid protein was depressed by the chronic treatment. On the other hand, the amount of iodocompound released by the autoproteolysis, which may reflect hormone secretion, increased, possibly because of the marked increase in the iodine content of thyroglobulin.  (+info)

INTRATHYROIDAL IODINE METABOLISM IN THE RAT. THE INFLUENCE OF DIET AND THE ADMINISTRATION OF THYROID-STIMULATING HORMONE. (5/25)

1. Ratios of mono[(131)I]iodotyrosine and di[(131)I]iodotyrosine (R values) and the incorporation of (131)I into iodothyronines have been estimated in rat thyroid glands from 30min. to 38hr. after the administration of [(131)I]iodide. 2. In rats receiving a powdered low-iodine diet the R values were close to unity and did not change with time after the administration of [(131)I]iodide. In rats receiving a commercial pellet diet the R values fell from a mean of 0.8 at 30min. after [(131)I]iodide administration to 0.49 at 38hr. 3. Administration of 0.5-2.0i.u. of thyroid-stimulating hormone before giving the injection of [(131)I]iodide caused a small diminution in the R value when the time between injecting [(131)I]iodide and killing the animal was 16hr. or more. 4. Iodothyronines represented a greater percentage of the total thyroid-gland radioactivity in the iodine-deficient animals than in animals fed on the pellet diet. Thyroid-stimulating hormone had little effect, if any, on the iodothyronine contents.  (+info)

Studies on experimental iodine allergy: 1. Antigen recognition of guinea pig anti-iodine antibody. (6/25)

It has generally been thought that iodine allergy is cross-sensitive to various iodine-containing chemicals. However, this concept seems to deviate from the immunological principle that immune recognition is specific. To solve this contradiction, we hypothesize that iodine allergy is an immunological reaction to iodinated autologous proteins produced in vivo by iodination reaction from various iodine-containing chemicals. Antisera to iodine were obtained from guinea pigs immunized subcutaneously with iodine-potassium iodide solution emulsified in complete Freund's adjuvant (CFA). The specificity of guinea pig anti-iodine antiserum was determined by enzyme-linked immunosorbent assay (ELISA) inhibition experiments using microplates coated with iodinated guinea pig serum albumin (I-GSA). Antibody activities were inhibited by I-GSA, diiodo-L-tyrosine, and thyroxine, but not by potassium iodide, monoiodo-L-tyrosine, 3,5,3'-triiodothyronine, monoiodo-L-histidine, or diiodo-L-histidine, or by ionic or non-ionic iodinated contrast media. The results that antigen recognition of anti-iodine antibody is specific to iodinated protein support our hypothesis. While protein iodination usually takes place both at histidine residues as well as at tyrosine residues, only iodinated tyrosine acted as an antigenic determinant and no antibody activities to iodinated histidine were detected in our experimental iodine allergy model.  (+info)

Studies on experimental iodine allergy: 3. Low molecular weight elicitogenic antigens of iodine allergy. (7/25)

We hypothesize that iodine allergy is an immune response to iodinated self proteins produced in vivo from various iodine-containing chemicals. Since an antigenic determinant of experimental iodine allergy is diiodotyrosine (DIT), we designed low molecular weight DIT derivatives having provocative antigenicity without sensitizing immunogenicity. Tetraiododityrosine and hexaiodotrityrosine provoked dose-dependent skin reactions in guinea pigs previously immunized with iodine. No guinea pigs immunized with hexaiodotrityrosine showed anaphylactic reaction by i.v. challenge with hexaiodotrityrosine and none of their antisera showed positive passive cutaneous anaphylaxis (PCA) reaction in guinea pigs, indicating the non-immunogenic nature of the compound. Erythrosine, one of the color additives having a structure common with DIT, was assessed for its immunological property. Enzyme-linked immunosorbent assay (ELISA) inhibition studies on erythrosine revealed that the inhibitory activity of erythrosine was stronger than that of DIT. Furthermore, erythrosine provoked a PCA reaction in animals sensitized with anti-iodine antisera. In conclusion, hexaiodotrityrosine is thought to be useful for skin testing of iodine allergy without any fear of sensitization to the allergen. Erythrosine was shown to provoke an experimental iodine allergy and, also, the relationships between the new concept of iodine allergy and features of clinical findings of adverse effects by iodocontrast media are discussed.  (+info)

Deciphering the peptide iodination code: influence on subsequent gas-phase radical generation with photodissociation ESI-MS. (8/25)

 (+info)

Diiodotyrosine (DIT) is a thyroid hormone precursor that contains two iodine atoms and the amino acid tyrosine. It is formed in the thyroid gland by the enzymatic iodination of tyrosine residues within the thyroglobulin protein. DIT can then be further combined and processed to form the active thyroid hormones triiodothyronine (T3) and thyroxine (T4), which contain three and four iodine atoms, respectively.

In summary, Diiodotyrosine is an essential intermediate in the synthesis of thyroid hormones T3 and T4.

Monoiodotyrosine (MIT) is a thyroid hormone precursor that is formed by the iodination of the amino acid tyrosine. It is produced in the thyroid gland as part of the process of creating triiodothyronine (T3) and thyroxine (T4), which are active forms of thyroid hormones. MIT itself does not have significant biological activity, but it plays a crucial role in the synthesis of more important thyroid hormones.

Lactoperoxidase is a type of peroxidase enzyme that is present in various secretory fluids, including milk, saliva, and tears. In milk, lactoperoxidase plays an important role in the natural defense system by helping to protect against microbial growth. It does this by catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which is a potent antimicrobial agent.

Lactoperoxidase is a glycoprotein with a molecular weight of approximately 78 kDa, and it is composed of four identical subunits, each containing a heme group that binds to the hydrogen peroxide molecule during the enzymatic reaction. Lactoperoxidase has been studied for its potential therapeutic applications in various fields, including oral health, food preservation, and wound healing.

I couldn't find a medical definition for "Ampyrone" as it is not a recognized or commonly used term in medicine or pharmacology. It may be possible that you have made a slight error in the spelling, and you are actually looking for "Amiodarone," which is a medication used to treat and prevent various types of heart rhythm disorders.

If this is not the case, please provide more context or clarify your question so I can give you an accurate answer.

Iodides are chemical compounds that contain iodine in the form of an iodide ion (I-). Iodide ions are negatively charged ions that consist of one iodine atom and an extra electron. Iodides are commonly found in dietary supplements and medications, and they are often used to treat or prevent iodine deficiency. They can also be used as expectorants to help thin and loosen mucus in the respiratory tract. Examples of iodides include potassium iodide (KI) and sodium iodide (NaI).

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.

Thyroglobulin is a protein produced and used by the thyroid gland in the production of thyroid hormones, primarily thyroxine (T4) and triiodothyronine (T3). It is composed of two subunits, an alpha and a beta or gamma unit, which bind iodine atoms necessary for the synthesis of the thyroid hormones. Thyroglobulin is exclusively produced by the follicular cells of the thyroid gland.

In clinical practice, measuring thyroglobulin levels in the blood can be useful as a tumor marker for monitoring treatment and detecting recurrence of thyroid cancer, particularly in patients with differentiated thyroid cancer (papillary or follicular) who have had their thyroid gland removed. However, it is important to note that thyroglobulin is not specific to thyroid tissue and can be produced by some non-thyroidal cells under certain conditions, which may lead to false positive results in some cases.

Goiter is a medical term that refers to an enlarged thyroid gland. The thyroid gland is a small, butterfly-shaped gland located in the front of your neck below the larynx or voice box. It produces hormones that regulate your body's metabolism, growth, and development.

Goiter can vary in size and may be visible as a swelling at the base of the neck. It can be caused by several factors, including iodine deficiency, autoimmune disorders, thyroid cancer, pregnancy, or the use of certain medications. Depending on the underlying cause and the severity of the goiter, treatment options may include medication, surgery, or radioactive iodine therapy.

The thyroid gland is a major endocrine gland located in the neck, anterior to the trachea and extends from the lower third of the Adams apple to the suprasternal notch. It has two lateral lobes, connected by an isthmus, and sometimes a pyramidal lobe. This gland plays a crucial role in the metabolism, growth, and development of the human body through the production of thyroid hormones (triiodothyronine/T3 and thyroxine/T4) and calcitonin. The thyroid hormones regulate body temperature, heart rate, and the production of protein, while calcitonin helps in controlling calcium levels in the blood. The function of the thyroid gland is controlled by the hypothalamus and pituitary gland through the thyroid-stimulating hormone (TSH).

Thyroid hormones are hormones produced and released by the thyroid gland, a small endocrine gland located in the neck that helps regulate metabolism, growth, and development in the human body. The two main thyroid hormones are triiodothyronine (T3) and thyroxine (T4), which contain iodine atoms. These hormones play a crucial role in various bodily functions, including heart rate, body temperature, digestion, and brain development. They help regulate the rate at which your body uses energy, affects how sensitive your body is to other hormones, and plays a vital role in the development and differentiation of all cells of the human body. Thyroid hormone levels are regulated by the hypothalamus and pituitary gland through a feedback mechanism that helps maintain proper balance.

... transaminase Dème D, Fimiani E, Pommier J, Nunez J (February 1975). "Free diiodotyrosine effects on protein ... Diiodotyrosine (DIT) is a precursor in the production of thyroid hormone, and results from iodization of monoiodotyrosine at ... when diiodotyrosine is combined with monoiodotyrosine (in the colloid of the thyroid follicle). Two molecules of DIT combine to ...
In enzymology, a diiodotyrosine transaminase (EC 2.6.1.24) is an enzyme that catalyzes the chemical reaction 3,5-diiodo-L- ... Other names in common use include diiodotyrosine aminotransferase, halogenated tyrosine aminotransferase, and halogenated ...
To combat this issue, a sensitive assay has recently been created that measures the amounts of mono- and diiodotyrosine in the ... Di-iodotyrosine deshalogenating activity of human thyroid tissue". The Journal of Clinical Endocrinology and Metabolism. 16 (8 ... Iodotyrosine deiodinase is located on the apical plasma membrane of the thyroid colloid, where mono- and diiodotyrosine are ... Within the thyroid follicular cell, thyroglobulin is hydrolyzed to form thyroid hormones and mono- and diiodotyrosine. The ...
The formation of thyroxine and diiodotyrosine by the completely thyroidectomized animal". J. Biol. Chem. 147: 757-769. doi: ...
The iodination of specific tyrosines yields monoiodotyrosine (MIT) and diiodotyrosine (DIT). One MIT and one DIT are ...
This forms the precursors of thyroid hormones monoiodotyrosine (MIT), and diiodotyrosine (DIT). When the follicular cells are ...
Nature of a thyroxine precursor formed in the synthesis of thyroxine from diiodotyrosine and its keto acid analog". ... Plants, insects, zooplankton and algae store iodine as mono-iodotyrosine (MIT), di-iodotyrosine (DIT), iodocarbons, or ... Nonenzymic formation of 3,5,3'-triiodothyronine from 4-hydroxy-3-iodophenylpyruvic acid, 3,5-diiodotyrosine, and oxygen". ...
One unit can combine with diiodotyrosine to form triiodothyronine, as occurs in the colloid of the thyroid follicle. Two units ...
... of moral reasoning Dietary induced thermogenesis Diiodotyrosine, a chemical compound Dual inheritance theory Digital ion trap ...
... diiodotyrosine MeSH D12.125.072.050.875.379 - melanins MeSH D12.125.072.050.875.496 - monoiodotyrosine MeSH D12.125.072.050. ...
... diiodotyrosine transaminase EC 2.6.1.25: deleted, Now included with EC 2.6.1.24 diiodotyrosine transaminase EC 2.6.1.26: ...
... diiodotyrosine MeSH D06.472.931.388 - monoiodotyrosine MeSH D06.472.931.669 - thyroid gland, desiccated MeSH D06.472.931.740 - ...
... combinations H03BC01 Potassium perchlorate H03BX01 Diiodotyrosine H03BX02 Dibromotyrosine "ATC (Anatomical Therapeutic Chemical ...
Diiodotyrosine transaminase Dème D, Fimiani E, Pommier J, Nunez J (February 1975). "Free diiodotyrosine effects on protein ... Diiodotyrosine (DIT) is a precursor in the production of thyroid hormone, and results from iodization of monoiodotyrosine at ... when diiodotyrosine is combined with monoiodotyrosine (in the colloid of the thyroid follicle). Two molecules of DIT combine to ...
3,5-Diiodotyrosine;a precursor of thyroxine. iodohippurate sodium (i-o′do-hip′poo-rat). A radiopaque compound formerly used ...
Two molecules of di-iodotyrosine combine to form T4, and one molecule of mono-iodotyrosine combines with one molecule of di- ... Iodination of tyrosine forms mono-iodotyrosine and di-iodotyrosine. ...
How much do you know about BRS endocrine physiology? Do you think you can pass this quiz? This quiz shows a graph for several questions. You must look at the gr...
MHC Class I in complex with modified Sendai virus nucleoprotein peptide FAPGN(3,5-diiodotyrosine)PAL Coordinates. PDB Format ...
T4 contains four iodine atoms and is formed by the coupling of two molecules of diiodotyrosine (DIT). T3 contains three atoms ...
"The salivary glands deiodinate thyroxine and return the iodine to the thyroid gland as diiodotyrosine." (90% in 20 minutes in ... The thyroglobulin (the normal hormone) can be split into thyroxine and di-iodotyrosine. Both individually will promote the ... and returned to the thyroid as diiodotyrosine, where the thyroxine is regenerated. ...
This protein contains Thyroxin, Diiodotyrosine & Triiodothyronine in different proportion. -Excretion mainly through Kidney. ...
... of sulfanilamide-like compounds as inhibitors of the invitro conversion of inorganic iodide to thyroxine and diiodotyrosine by ... of sulfanilamide-like compounds as inhibitors of the invitro conversion of inorganic iodide to thyroxine and diiodotyrosine by ... of sulfanilamide-like compounds as inhibitors of the invitro conversion of inorganic iodide to thyroxine and diiodotyrosine by ...
This keeps the quantity of thyroglobulin low, a mixture of diiodotyrosine and de thyroxine. All the functions of this gland are ... In fact, it has been possible to extract triiodothyronine, thyroglobulin, thyroxine, and lately diiodotyrosine, which appear to ... be the chemical skeleton of diiodotyrosine, the one that seems to be the true hormone, THYROXINE. This is a white, insipid ...
... and diiodotyrosine (DIT). Thyroxine is produced by linking two moieties of DIT. Combining one particle of MIT and one particle ...
Tyrosine in contact with the membrane of the follicular cells is iodinated at 1 (monoiodotyrosine) or 2 (diiodotyrosine) sites ...
DIT: diiodotyrosine. ERK: extracellular signal-regulated kinase. GPCR: G protein-coupled receptor ...
Diiodotyrosine. 90mcg. **. Iodotyrosine. 50mcg. **. This product has been distributed by a NSF Good Manufacuring Practices (GMP ...
... and diiodotyrosine (DIT) and then T3 and T4), we hypothesized that by searching the presence of perfect or imperfect versions ...
Diiodotyrosine Receptors. MIT Receptors. Monoiodotyrosine Receptors. Receptors, DIT. Receptors, Diiodotyrosine. Receptors, MIT ...
Thyroid glands produce diiodotyrosine. Literature cited: Veldhuis, Froona, Embryonic development day 11-14, Sept 15, 2008 http ...
... addition of a second iodine atom produces diiodotyrosine. A monoiodotyrosine and diiodotyrosine combine to form ... Addition of one iodine atom creates monoiodotyrosine, and the addition of a second iodine creates diiodotyrosine. Two of these ... The combination of a monoiodotyrosine and a diiodotyrosine yields triiodothyronine, and the combination of two diiodotyrosines ...
O-(4-Hydroxy-3,5-diiodophenyl)-3,5-diiodotyrosine Term UI T040988. Date03/16/1995. LexicalTag NON. ThesaurusID NLM (1996). ... O-(4-Hydroxy-3,5-diiodophenyl)-3,5-diiodotyrosine Oroxine Sodium Levothyroxine Synthroid Synthrox T4 Thyroid Hormone Thevier ... Thyroxine is synthesized via the iodination of tyrosines (MONOIODOTYROSINE) and the coupling of iodotyrosines (DIIODOTYROSINE) ... Thyroxine is synthesized via the iodination of tyrosines (MONOIODOTYROSINE) and the coupling of iodotyrosines (DIIODOTYROSINE) ...
Thyroxine is synthesized via the iodination of tyrosines (monoiodotyrosine) and the coupling of iodotyrosines (diiodotyrosine) ...
Organification is the largely self-regulated process; iodide is integrated into monoiodotyrosine (MIT) or diiodotyrosine (DIT) ...
Thus, mono-iodotyrosine (MIT) and di-iodotyrosine (DIT) are produced.. thyroid hormone synthesis. ...
Monoiodotyrosine is one iodine attached to a tyrosine backbone and diiodotyrosine contains 2 iodines attached to a tyrosine ... These small halves of thyroid hormone are called monoiodotyrosine (3) and diiodotyrosine. ... hormone or it can smash 1 diiodotyrosine and 1 monoiodotyrosine (1 iodine + 2 iodines means 3 iodines total) together to form ...
This results in the formation of monoiodotyrosine (MIT) and diiodotyrosine (DIT), iodinated tyrosine derivatives[8]. ...
The first product is monoiodotyrosine (MIT). MIT is next iodinated on the carbon 5 position to form diio-dotyrosine (DIT). Two ...
Iodine is taken up by the thyroid gland and converted to diiodotyrosine and thyroxine. ...
  • Diiodotyrosine (DIT) is a precursor in the production of thyroid hormone, and results from iodization of monoiodotyrosine at the other meta- position on the phenol ring. (wikipedia.org)
  • Triiodothyronine is formed, when diiodotyrosine is combined with monoiodotyrosine (in the colloid of the thyroid follicle). (wikipedia.org)
  • Via a reaction with the enzyme thyroperoxidase, iodine is covalently bound to tyrosine residues in thyroglobulin molecules, forming monoiodotyrosine (MIT) and diiodotyrosine (DIT). (loinc.org)
  • Tyrosine in contact with the membrane of the follicular cells is iodinated at 1 (monoiodotyrosine) or 2 (diiodotyrosine) sites and then coupled to produce the 2 forms of thyroid hormone. (msdmanuals.com)
  • Addition of one iodine atom creates monoiodotyrosine, and the addition of a second iodine creates diiodotyrosine. (mhmedical.com)
  • The combination of a monoiodotyrosine and a diiodotyrosine yields triiodothyronine, and the combination of two diiodotyrosines yields thyroxine. (mhmedical.com)
  • A monoiodotyrosine and diiodotyrosine combine to form triiodothyronine (T 3 ). (mhmedical.com)
  • Thyroxine is synthesized via the iodination of tyrosines ( MONOIODOTYROSINE ) and the coupling of iodotyrosines ( DIIODOTYROSINE ) in the THYROGLOBULIN . (nih.gov)
  • Some tyrosine residues are bound by only one iodine, whereas others are bound by two iodine atoms , yielding monoiodotyrosine or MIT, and diiodotyrosine or DIT, respectively. (osmosis.org)
  • Antithyroid drugs such as the thiourea group inhibit iodide oxidation and therefore its subsequent incorporation into monoiodotyrosine (MIT) and diiodotyrosine (DIT). (medscape.com)
  • As to the thyroid precursor molecules, diiodotyrosine (DIT) and monoiodotyrosine (MIT), both human and Xenopus mct8, showed active efflux, but no influx. (researcher-app.com)
  • The structural specificity of sulfanilamide-like compounds as inhibitors of the invitro conversion of inorganic iodide to thyroxine and diiodotyrosine by thyroid tissue. (safecosmetics.org)
  • T4 contains four iodine atoms and is formed by the coupling of two molecules of diiodotyrosine (DIT). (rxlist.com)
  • addition of a second iodine atom produces diiodotyrosine. (mhmedical.com)
  • Iodotyrosine deiodinase facilitates iodide salvage in the thyroid by catalyzing deiodination of mono - and diiodotyrosine , the halogenated byproducts of thyroid hormone production. (wikidoc.org)
  • This gene encodes an enzyme that catalyzes the oxidative NADPH-dependent deiodination of mono- and diiodotyrosine, which are the halogenated byproducts of thyroid hormone production. (nih.gov)
  • [16] Iodotyrosine deiodinase is located on the apical plasma membrane of the thyroid colloid, where mono- and diiodotyrosine are produced from this breakdown of thyroglobulin. (wikidoc.org)
  • Within the thyroid follicular cell, thyroglobulin is hydrolyzed to form thyroid hormones and mono- and diiodotyrosine. (wikidoc.org)