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What molecule holds onto oxygen in blood cells?
Hemoglobin is the molecule responsible for holding onto oxygen in red blood cells. It is a protein that contains iron and is essential for oxygen transport in the bloodstream.
The bright red color of skeletal muscle is due mainly to its?
rich supply of myoglobin, a protein that stores oxygen in muscle cells. Myoglobin has a deep red color when exposed to oxygen, giving skeletal muscle its distinctive hue.
What is the percent similarity of myoglobin and hemoglobin How much are they alike?
Myoglobin and hemoglobin are structurally similar proteins, with around 20% sequence similarity. They both contain heme groups that bind oxygen, but hemoglobin is found in red blood cells and is responsible for transporting oxygen, while myoglobin is found in muscle tissue and is involved in storing and transporting oxygen within muscles.
What best describes the shape of myoglobin which is many ways is a typical protein?
Myoglobin is typically described as a globular protein due to its compact, spherical shape. It is made up of a single polypeptide chain folded into a three-dimensional structure that allows it to bind and store oxygen in muscle tissues. This shape enables myoglobin to perform its function efficiently within muscle cells.
What color is haemoglobin?
Hemoglobin is red in color when it is carrying oxygen.
What is myoglobulinemia?
You have a myoglobin, an oxygen storage molecule akin to haemoglobin, in the blood. This could be due to the muscle trauma or ischaemia leading to death and breakdown. Myoglobin is toxic to kidney nephrons.
Why hemoglobin is better long distance oxygen transporter than myoglobin?
Hemoglobin has four binding sites for oxygen, allowing it to transport more oxygen compared to myoglobin, which has only one binding site. Additionally, hemoglobin releases oxygen under lower partial pressures, making it more efficient for delivering oxygen to tissues during long distances. Myoglobin is mainly found in muscle cells and is better suited for short bursts of oxygen storage.
What is the difference between Haemoglobin and Hematic?
Haemoglobin is the red pigment found in Erythrocytes which is responsible for transfer of Oxygen. Hematic is the adjective which means related to blood.
Is there any difference in hemoglobin?
haemoglobin
Why are slow twitch fibers re in colour and why are fast twitch fibers white?
Presence of myoglobin makes the difference between the two.
What's the difference between white meat and dark meat in poultry?
The main difference between white meat and dark meat in poultry is the amount of myoglobin, a protein that stores oxygen in muscles. White meat has less myoglobin and is found in muscles that are used for quick bursts of activity, like the breast. Dark meat has more myoglobin and is found in muscles that are used for sustained activity, like the legs and thighs. This difference in muscle usage affects the flavor, texture, and nutritional content of the meat.
How can the oxygen store in myoglobin be replaced after use?
The oxygen store in myoglobin can be replenished by diffusion from the bloodstream, where oxygen is carried by hemoglobin. When myoglobin releases oxygen to the muscle cells for energy production, it becomes deoxygenated, creating a concentration gradient that drives the diffusion of oxygen back into myoglobin. This process allows myoglobin to continuously store and release oxygen as needed by the muscle cells.
What's the difference between dark meat and white meat in poultry?
The main difference between dark meat and white meat in poultry is the amount of myoglobin present in the muscle. Dark meat has more myoglobin, which gives it a darker color and a richer flavor compared to white meat. Additionally, dark meat tends to be juicier and more tender due to its higher fat content.
What make the skeletal muscle bright red?
Because muscles need a lot of ATP for muscle contraction and it needs oxygen to make ATP, it has its own form of hemoglobin called myoglobin. The binding of oxygen to hemo(myo)globin is what gives the characteristic red color in both RBCs and muscle tissue.
What type of proteins require a covalent bonded prosthetic group to function properly?
Proteins such as haemoglobin and myoglobin which require haem groups covalently bonded to the proximal histidine (HisF8) residue for O2 binding.
Is a protein a monomer?
No, proteins are made up of amino acids. Yes, at a larger scale, some proteins are monomers, made up of a single chain of amino acids, without a quaternary structure. Myoglobin is an example. About 80 % of the proteins, however, do have a quaternary structure. Haemoglobin, for example, is made up of four subunits similar to myoglobin.
Haemoglobin in percentage?
In percentage of what in what species, or objects. It is 0% in water! The percentage will depend on what the denominator is. there will be a huge difference between haemoglobin as a percentage of total blood or percentage of total body mass. Also it will vary: people living at high altitudes tend to have higher concentrations.
