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The colour blood red is a dark shade of the colour red meant to resemble the colour of human blood (which is composed of oxygenated red erythrocytes, white leukocytes, and yellow blood plasma). [2] It is the iron in hemoglobin specifically that gives blood its red colour.
Methemoglobinemia, or methaemoglobinaemia, is a condition of elevated methemoglobin in the blood. [2] Symptoms may include headache, dizziness, shortness of breath, nausea, poor muscle coordination, and blue-colored skin (cyanosis). [2]
Livor mortis (from Latin līvor 'bluish color, bruise' and mortis 'of death'), postmortem lividity (from Latin post mortem 'after death' and lividitas 'black and blueness'), hypostasis (from Greek ὑπό (hypo) 'under, beneath' and στάσις (stasis) 'a standing') [1] [2] or suggillation, is the second stage of death and one of the signs of ...
The disorder can cause heart abnormalities and seizures if the amount of methemoglobin in the blood exceeds 20 percent, but at levels between 10 and 20 percent it can cause blue skin without other symptoms. Most of the Fugates lived long and healthy lives. The "bluest" of the blue Fugates, Luna Stacy, had 13 children and lived to age 84. [6]
They appear as dense, blue-purple granules within the red blood cell and there are usually only one or two, located in the cell periphery. They stain on a Romanowsky stain because clumps of ribosomes are co‐precipitated with the iron‐containing organelles. A cell containing Pappenheimer bodies is a siderocyte.
Cyanosis is the change of body tissue color to a bluish-purple hue, as a result of decrease in the amount of oxygen bound to the hemoglobin in the red blood cells of the capillary bed. [1] Cyanosis is apparent usually in the body tissues covered with thin skin , including the mucous membranes , lips, nail beds , and ear lobes. [ 1 ]
The structure of cytochrome b5 reductase, the enzyme that converts methemoglobin to hemoglobin. [1]Methemoglobin (British: methaemoglobin, shortened MetHb) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe 3+ state, not the Fe 2+ of normal hemoglobin.
The purple coloring is caused by hemocyanin. Spectroscopy of oxyhemocyanin shows several salient features: [21] Resonance Raman spectroscopy shows that O 2 is bound in a symmetric environment (ν(O-O) is not IR-allowed). OxyHc is EPR-silent indicating the absence of unpaired electrons; Infrared spectroscopy shows ν(O-O) of 755 cm −1