Proteins are macromolecules making up the bulk of the body. Protein has a very important role in the function and structure of all living cells. This is because the protein molecule contains oxygen, carbon, nitrogen, hydrogen, and sulfur. Some proteins also contain phosphorus.
The benefits of protein for our body are numerous. Protein greatly affect the growth process of our body. Among the benefits of these proteins are as follows:
As the enzyme. The protein has a major role to speed up biological reactions.
As a means of transport and storage.
For Supporting mechanical. One form of protein fibers called collagen has a function to keep the strength and durability of bone and skin.
Defense Sebagau body or the body of Defense immunization. These proteins are commonly used in the form of antibodies.
As media propagation of nerve impulses.
As a growth control
And on the topic we will discuss about the transporter protein to accelerate biological reactions. Protein in hemoglobin to transport oxygen in the erythrocytes. The protein contained in myoglobin can transport oxygen in the muscles.
Hemoglobin is the iron-containing oxygen in the hemoglobin of red blood cells in the blood that carries oxygen from the respiratory organs (lungs) to the body (ie the tissues) where it releases the oxygen to burn nutrients to provide energy for the functioning of the organism, and collect the resulting carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.
In mammals, the protein makes up about 97% of the dry content of red blood cells', and about 35% of the total content (including water). Hemoglobin oxygen binding capacity 1.34 ml O2 per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared with the dissolved oxygen in the blood. Mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.
Hemoglobin is involved in the transport of other gases: it carries some body breathing carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the protein globin. This molecule also carries nitric oxide molecules important regulatory protein globin bound to the thiol group, releasing it at the same time with oxygen.
Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, and mesangial cells in the kidney. In the network, the function of hemoglobin has non-oxygen-carrying as an antioxidant and regulator of iron metabolism
Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In organisms, hemoglobin can carry oxygen, or they can act to transport and regulate other things such as carbon dioxide, nitrous oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge the oxygen away from the anaerobic system, such as nitrogen nodules of leguminous plants, before the oxygen can be toxic to the system.
Myoglobin (abbreviated Mb) is a single-chain protein is round 153 or 154 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which folds Apoprotein left. It has eight alpha helical hydrophobic core. It has a molecular weight of 17,699 dalton (with heme), and is the primary oxygen-carrying pigment of muscle tissue contrast to blood-borne hemoglobin., Which are structurally related to, this protein does not show cooperative binding of oxygen, since positive cooperativity belongs multimeric protein / oligomer only. A high concentration of myoglobin in muscle cells allow organisms to hold their breath again. Diving mammals such as whales and seals have muscles with very high abundance of myoglobin.
Myoglobin was the first protein to have a three-dimensional structure revealed In 1958, John Kendrew and colleagues successfully determined the structure of myoglobin by high-resolution X-ray crystallography .. For this discovery, John Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz Despite being one of the most studied proteins in biology, the true physiological function has yet to convince established: mice genetically engineered to lack a decent myoglobin, but showed a 30% reduction in heart. Systolic output. They are adapted to this deficiency through genetic mechanisms of hypoxia and increased vasodilation. In human myoglobin encoded by MB
Ceruloplasmin
Ceruloplasmin is a copper enzyme with a substance that serves as a catalyst in organic reactions
4 Fe2 + + 4 H + + O2 <=> 4 Fe3 + + 2 H2O
Ceruloplasmin enzyme activity has ferrioxidase that converts iron iron in the form of cells and in the form of a store with transferrin and ultimately used by the bone marrow to the manufacturing process of erythrocytes. Ceruloplasmin is the main form of the copper minerals are present in the circulation of the blood (plasma). Forms of Cu in the body bind to a complex protein that is 90% globulin bound in the form of ceruloplasmin and 10% by albumin. Ceruloplasmin have activity as an enzyme capable of converting ferroksidase ferrous iron in the form of the cells and in the form of a store with transferring and ultimately used by the bone marrow to the process of making erythrocytes (erytropoiesis). Ceruloplasmin is α-2-globulin. This protein is blue because it contains copper and carry 90% of the copper present in the plasma. Myoglobin myoglobin is a protein that is a constituent of the blood that binds oxygen. Suitable as a carrier protein myoglobin oxygen, but it is effective as an oxygen storage protein. Myoglobin in red muscle tissue that binds oxygen in the protein Myoglobin is an iron-and oxygen-binding was found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is an iron-and protein-binding oxygen in the blood, especially red blood cells. The only time myoglobin is found in the bloodstream is when it is released after muscle injury. This is an abnormal finding, and diagnosis can be relevant when found in the blood
The benefits of protein for our body are numerous. Protein greatly affect the growth process of our body. Among the benefits of these proteins are as follows:
As the enzyme. The protein has a major role to speed up biological reactions.
As a means of transport and storage.
For Supporting mechanical. One form of protein fibers called collagen has a function to keep the strength and durability of bone and skin.
Defense Sebagau body or the body of Defense immunization. These proteins are commonly used in the form of antibodies.
As media propagation of nerve impulses.
As a growth control
And on the topic we will discuss about the transporter protein to accelerate biological reactions. Protein in hemoglobin to transport oxygen in the erythrocytes. The protein contained in myoglobin can transport oxygen in the muscles.
Hemoglobin is the iron-containing oxygen in the hemoglobin of red blood cells in the blood that carries oxygen from the respiratory organs (lungs) to the body (ie the tissues) where it releases the oxygen to burn nutrients to provide energy for the functioning of the organism, and collect the resulting carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.
In mammals, the protein makes up about 97% of the dry content of red blood cells', and about 35% of the total content (including water). Hemoglobin oxygen binding capacity 1.34 ml O2 per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared with the dissolved oxygen in the blood. Mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.
Hemoglobin is involved in the transport of other gases: it carries some body breathing carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the protein globin. This molecule also carries nitric oxide molecules important regulatory protein globin bound to the thiol group, releasing it at the same time with oxygen.
Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, and mesangial cells in the kidney. In the network, the function of hemoglobin has non-oxygen-carrying as an antioxidant and regulator of iron metabolism
Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In organisms, hemoglobin can carry oxygen, or they can act to transport and regulate other things such as carbon dioxide, nitrous oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge the oxygen away from the anaerobic system, such as nitrogen nodules of leguminous plants, before the oxygen can be toxic to the system.
Myoglobin (abbreviated Mb) is a single-chain protein is round 153 or 154 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which folds Apoprotein left. It has eight alpha helical hydrophobic core. It has a molecular weight of 17,699 dalton (with heme), and is the primary oxygen-carrying pigment of muscle tissue contrast to blood-borne hemoglobin., Which are structurally related to, this protein does not show cooperative binding of oxygen, since positive cooperativity belongs multimeric protein / oligomer only. A high concentration of myoglobin in muscle cells allow organisms to hold their breath again. Diving mammals such as whales and seals have muscles with very high abundance of myoglobin.
Myoglobin was the first protein to have a three-dimensional structure revealed In 1958, John Kendrew and colleagues successfully determined the structure of myoglobin by high-resolution X-ray crystallography .. For this discovery, John Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz Despite being one of the most studied proteins in biology, the true physiological function has yet to convince established: mice genetically engineered to lack a decent myoglobin, but showed a 30% reduction in heart. Systolic output. They are adapted to this deficiency through genetic mechanisms of hypoxia and increased vasodilation. In human myoglobin encoded by MB
Ceruloplasmin
Ceruloplasmin is a copper enzyme with a substance that serves as a catalyst in organic reactions
4 Fe2 + + 4 H + + O2 <=> 4 Fe3 + + 2 H2O
Ceruloplasmin enzyme activity has ferrioxidase that converts iron iron in the form of cells and in the form of a store with transferrin and ultimately used by the bone marrow to the manufacturing process of erythrocytes. Ceruloplasmin is the main form of the copper minerals are present in the circulation of the blood (plasma). Forms of Cu in the body bind to a complex protein that is 90% globulin bound in the form of ceruloplasmin and 10% by albumin. Ceruloplasmin have activity as an enzyme capable of converting ferroksidase ferrous iron in the form of the cells and in the form of a store with transferring and ultimately used by the bone marrow to the process of making erythrocytes (erytropoiesis). Ceruloplasmin is α-2-globulin. This protein is blue because it contains copper and carry 90% of the copper present in the plasma. Myoglobin myoglobin is a protein that is a constituent of the blood that binds oxygen. Suitable as a carrier protein myoglobin oxygen, but it is effective as an oxygen storage protein. Myoglobin in red muscle tissue that binds oxygen in the protein Myoglobin is an iron-and oxygen-binding was found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is an iron-and protein-binding oxygen in the blood, especially red blood cells. The only time myoglobin is found in the bloodstream is when it is released after muscle injury. This is an abnormal finding, and diagnosis can be relevant when found in the blood
Hemoglobin is an iron-rich protein in red blood cells and functioning is essential for transporting oxygen from the lungs to all parts of the body that need it for energy. If the hemoglobin production is reduced or absent, then supply the energy needed for the functioning of the body can not be met, so that the body functions was disrupted and no longer able to carry out normal activities and cause decreased protein hemoglobin grade disease called hemoglobinopathy, among which the most common is sickle cell anemia or thalassemia. This disease, a disorder of red blood cells which is the result of an imbalance of the creation of one of the four amino acid chains that make up hemoglobin. Thalassemia is a disease that are inherited. whereas hemoglobin also play an important role in maintaining the shape of red blood cells, hemoglobin here why not play it?
BalasHapusand why the opportunity to recover from sickle cell or thalassemia is still relatively small because the affected physical condition?
ok, i'll try to answer..
BalasHapusThalassemia is an inherited blood disorder or inherited condition characterized by red blood cells are easily damaged or flourescent (<120 days) so that patients have anemia and had to undergo blood transfusions for life
In thalassemia occurs abnormalities in genes that regulate the formation of the globin chains that production is disrupted. Disorders of globin chain formation will result in damage to the red blood cells that will eventually lead to rupture of the blood cells.
Well, why the disease is difficult to recover? I think the disease is a disease of the descendants ...
in thalassemia occurs abnormalities in genes that regulate the formation of the globin chains that production is disrupted. Disorders of globin chain formation will result in damage to the red blood cells that will eventually lead to rupture of the blood cells. so that hemoglobin can not take damage. possibility of full recovery is very small or no because it is a gene disorder
BalasHapusi will try to answer :
BalasHapusas we know the thalassemia occurs abnormalities in genes that regulate the formation of the globin chains that production is disrupted. Disorders of globin chain formation will result in damage to the red blood cells that will eventually lead to rupture of the blood cells. here i take the conclusions may not be able to perform its role of hemoglobin due to interference from thelemesia was very severe.