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Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. Nitric oxide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells. The latter reaction is a remnant activity of the more ancient nitric oxide dioxygenase function of globins.
A:Normal red blood cells are shown flowing freely in a blood vessel on the top of the diagram. The inset image shows a cross-section of a normal red blood cell with normal hemoglobin. B:Demonstrates abnormal, sickled red blood cells blocking blood flow in a blood vessel (vaso-occlusive crisis). The inset image shows a cross-section of a sickle ...
Myoglobin is found in Type I muscle, Type II A, and Type II B; although many older texts describe myoglobin as not found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. [14] Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography. [15]
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).
Hemoglobin is an iron-containing protein that gives red blood cells their color and facilitates transportation of oxygen from the lungs to tissues and carbon dioxide from tissues to the lungs to be exhaled. [3] Red blood cells are the most abundant cell in the blood, accounting for about 40–45% of its volume. Red blood cells are circular ...
Specifically, they recognize cell-surface glycoconjugates containing sialic acid on the surface of host red blood cells with a low affinity and use them to enter the endosome of host cells. [6] Hemagglutinins tend to recognize α-2,6-linked sialic acids of the host cells in humans and α-2,3-linked sialic acids in avian species, although there ...
Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia. [11] Neuroglobin belongs to a branch of the globin family that diverged early in evolution. Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to neuroglobin. [12]
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a