Ví dụ về việc sử dụng The heme trong Tiếng anh và bản dịch của chúng sang Tiếng việt
{-}
-
Colloquial
-
Ecclesiastic
-
Computer
The hemes use iron to bond to oxygen.
Meat, fish and poultry contain the heme form, which is easily absorbed by your body.
In animals, plants, and fungi,iron is often the metal ion incorporated into the heme complex.
Here Fe()-E represents the iron center of the heme group attached to the enzyme.
In the transportation or detection of diatomic gases,the gas binds to the heme iron.
These REV-ERBs are triggered by the heme group which is made up of tiny compounds that contain iron.
The heme is a molecule that makes up one of the two parts of a hemoglobin, which carries oxygen in the blood of animals.
This is a catalytic test that detects the heme group in blood that transports oxygen and carbon dioxide.
This is because they consume mainly non-heme iron,which is not absorbed as well as the heme form in animal products.
Binding sites for oxygen are the heme groups, the Fe++-porphyrin portions of the hemoglobin molecule.
It's estimated that 85- 90% of total iron intake comes from the non-heme form, while 10-15% comes from the heme form(3, 4).
They include the heme groups that are attached to the oxygen-carrying protein hemoglobin(shown in Figure 3.8).
Iron: Found in high amounts in beef,meat iron is mostly in the heme form, which is absorbed very efficiently.
Here, we can take the heme molecules from these waste products and use it for renewable energy storage.”.
Oxygen then bonds to the iron, and it is the interaction between the heme units and the oxygen that makes blood red.
For example, the ability of hemoglobin to effectively deliver oxygen to tissues isdue to amino acid residues located near the heme molecule.
Only about 2% to 20% of non-heme iron is absorbed,versus 15% to 35% of the heme iron found only in animal foods, specifically meat.
The heme portion of this hemoglobin molecule is then converted into bilirubin, which is transported in the bloodstream to the liver for further metabolism and excretion.
Raw Letrozole powder blocks production of estrogens in this way by competitive,reversible binding to the heme of its cytochrome P450 unit.
First the hemoglobin gets stripped of the heme molecule which thereafter passes through various processes of porphyrin catabolism, depending on the part of the body in wh….
Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix.
In biology, carbon monoxide is naturally produced by the action of heme oxygenase 1 and2 on the heme from hemoglobin breakdown.
Hb consists of the heme group, which is formed by iron, and globine chains, which can be alpha, beta, gamma or delta, resulting in the main types of hemoglobin, such as: HbA1, which is formed by two alpha chains and two beta chains and is present in higher concentration in blood;
Each type of AHP results from a geneticdefect leading to deficiency in one of the enzymes of the heme biosynthesis pathway in the liver.
The iron atom in heme binds to the 4 nitrogen atoms in the centre of the porphyrin ring, but this leaves two free bonding sites for the iron,one on either side of the heme plane.
In these two examples, a metal is complexed at the center of a tetrapyrrole macrocycle ring:the metal being iron in the heme group(iron in a porphyrin ring) of hemoglobin, or magnesium complexed in a chlorin-type ring in the case of chlorophyll.
Methylene blue, when injected intravenously as an antidote, is itself first reduced to leucomethylene blue,which then reduces the heme group from methemoglobin to hemoglobin.
Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning the iron is not completely oxidized to+V,but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation(.+).
Elevated levels of methemoglobin in the blood are caused when the mechanisms that defend against oxidative stress within the red blood cell are overwhelmed andthe oxygen carrying ferrous ion(Fe2+) of the heme group of the hemoglobin molecule is oxidized to the ferric state(Fe3+).