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Which part o the hemoglobin molecule does carbon dioxide attach?
Carbon dioxide primarily binds to the globin part of the hemoglobin molecule, specifically to specific amino acid residues within the globin chains. This binding forms carbaminohemoglobin and plays a role in the transport of carbon dioxide from tissues to the lungs for elimination.
Two alpha chains and two gamma chains make up the protein globin part of?
Two alpha chains and two gamma chains make up the protein globin part of fetal hemoglobin (HbF). This type of hemoglobin is predominant in fetuses and newborns, and has a higher affinity for oxygen than adult hemoglobin (HbA), allowing for efficient oxygen transfer across the placenta.
Several of the different globin genes are expressed in humans but at different times in development what mechanism could allow for this?
The regulation of globin gene expression during development is controlled by changes in the chromatin structure and interactions with transcription factors. Specific DNA sequences within the globin gene promoters and enhancers play a role in determining when and where these genes are expressed. Epigenetic modifications, such as DNA methylation and histone acetylation, also influence the timing of globin gene expression during development.
Why and hpw RBCs die?
RBC's die because they eject their nucleus during their formation in order to make more room for hemoglobin. Without a nucleus they are unable to make repairs and due to the stresses of traveling within the cardiovascular system. As a result they last on average about 120 days.Worn out RBC's are removed from circulation in the spleen and liver. The heme and globin portions of hemoglobin are split apart. The globin is broken down into amino acids which can be used to synthesize other proteins. Iron is removed from the heme portion and used to synthesize new heme molecules. The non-heme portion goes through a series of chemical transformations and eventually ends up as something called sterocobilin which is what gives feces it's characteristic brown color.
What vessels carry oxygen-rich blood throughout the body?
haemo globin carry oxygen to various parts of the body through blood
Does the hemoglobin molecule has polypeptide chains?
Yes. Hemoglobin consists of four heme groups as well as a globin. Globin is a type of protein - proteins are made of polypeptide chains.
Which Stains are used for staining globin chains of hemoglobin?
Hemoglobin electrophoresis uses stains such as Coomassie blue or Ponceau S to visualize the globin chains of the hemoglobin molecule. These stains help separate and identify different types of hemoglobin based on the migration pattern of the globin chains.
Which element is a major component of hemoglobin?
Haemoglobin is made up of a protein called globin which is bound to a red pigment called heme (hence the name haemoglobin) Globin is made up of 4 chains (polypeptide chains) embedded inside each of which is a heme molecule, the latter has an iron atom (in ferrous state) in it. It is the iron atom which carries a molecule of oxygen. As there are 4 chains this means that there are 4 iron atoms which means that 4 molecules of oxygen can be carried by each haemoglobin. Globulin
What is the iron-containing portion of the hemoglobin molecule called?
The iron containing part of hemoglobin is the 'heme' molecule.
What happens to the globin portion of the hemoglobin?
Nothing
Which part o the hemoglobin molecule does carbon dioxide attach?
Carbon dioxide primarily binds to the globin part of the hemoglobin molecule, specifically to specific amino acid residues within the globin chains. This binding forms carbaminohemoglobin and plays a role in the transport of carbon dioxide from tissues to the lungs for elimination.
Two alpha chains and two gamma chains make up the protein globin part of?
Two alpha chains and two gamma chains make up the protein globin part of fetal hemoglobin (HbF). This type of hemoglobin is predominant in fetuses and newborns, and has a higher affinity for oxygen than adult hemoglobin (HbA), allowing for efficient oxygen transfer across the placenta.
What does the medical terminology combining form -globin mean?
The medical terminology combining form -globin refers to a protein component found in hemoglobin. It is specifically related to the protein portion of hemoglobin molecules.
How many globin molecules are in each hemoglobin?
There are four nearly-identical individual protein chains in hemoglobin.
Hemoglobin is made up of the protein heme and the red pigment globin?
Hemoglobin is a protein found in red blood cells that functions to transport oxygen throughout the body. It is composed of a heme group, which contains iron and binds with oxygen, and globin chains, which provide the structure for the heme groups. The interaction between heme and globin allows hemoglobin to efficiently transport oxygen from the lungs to the body's tissues.
Does CO2 bind at the same site on the hemoglobin molecule as O2 If not where does CO2 bind?
No. Carbon monoxide binds to the same site as oxygen, i.e. the central iron. Carbon dioxide binds to the globin molecule.
Does oxytocin have a secondary structure or tertiary protein structure?
Yes it does. It also commonly contains quaternary structure.Secondary structure refers to folding and bonding interactions between atoms of the polypeptide backbone, either forming alpha-helices or Beta-sheets. Oxytocin contains both of these secondary structures as well as Beta-turns. Beta-sheets come in anti-parallel and parallel versions. Parallel means that the direction of the associated chains run in the same direction; N-terminus to C-terminus. Anti-parallel means that one or more of the associated chains run in an opposite direction to the others.Tertiary structure refers to interactions between side chains of the polypeptide residues. a good example of this is the disulfide bonds liking two cysteine residues which does occur in Oxytocin.Quaternary structure refers to association of separate polypeptide chains. Oxytocin can be found as a single chain in which case there is no quaternary structure. It is not uncommon however to find it as a pentamer, tetramer, or dimer. Conditions play a major factor in effecting its quaternary structure. whether it is in aqueous solution, biological conditions (cells), or crystallized. Another good example of quaternary structure is Hemoglobin. Hemoglobin is a dimer of dimers. 2 alpha-globin chains and 2 beta-globin chains.
