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OTHER WORDS FROM hemoglobinhe·mo·glo·bic, he·mo·glo·bin·ous, adjective
Words nearby hemoglobin
Example sentences from the Web for hemoglobin
At this pace, it will burn through its deep reserve of oxygen—provided by extra-large volumes of blood and hemoglobin—more slowly.
Targeting sickle hemoglobin directly has proved problematic given the large abundance of hemoglobin in the blood that would potentially require modification.Science Might Finally Have a Fix for This Rare Blood Disorder|Nick Fouriezos|December 15, 2020|Ozy
The next parameter is tissue oxygenation in the leg muscles, as measured with near-infrared spectroscopy, which basically involves shining infrared light through the skin and measuring how much is absorbed by oxygen-rich hemoglobin.How Does Your Brain Respond When You Hold Your Breath?|Alex Hutchinson|November 25, 2020|Outside Online
A single drop of a less-than-lily-white ancestral hemoglobin somewhere along the line?Six Fictional Marriages that Have Gone Very, Very Wrong|Jean Hanff Korelitz|March 25, 2014|DAILY BEAST
A red blood cell having no hemoglobin is also called a ghost.What's the Difference Between Ghouls, Goblins, and Ghosts?|Dictionary.com|November 1, 2010|DAILY BEAST
You can't fully understand how hemoglobin molecules interact until you've seen them depicted through a classical pas de deux.
In both conditions chemic tests will show hemoglobin, but in the latter the microscope will reveal the presence of red corpuscles.
In the lungs hemoglobin forms a loose combination with oxygen, which it readily gives up when it reaches the tissues.
Increase of hemoglobin, or hyperchromemia, is uncommon, and is probably more apparent than real.
Clinical study of the blood may be discussed under the following heads: I. Hemoglobin.
In mild cases a slight decrease of hemoglobin is the only blood change noted.
Medical definitions for hemoglobin
Scientific definitions for hemoglobin
A Closer Look
Ninety percent of the protein in red blood cells is made up of hemoglobin, the main oxygen transport molecule in mammals. A protein with four iron-containing subunits called hemes, hemoglobin is a complex molecule with a complex function. It must bind to oxygen in the lungs, then release that oxygen in the tissues, then bind to carbon dioxide in the tissues and release it in the lungs. Hemoglobin accomplishes oxygen transport by changing its structure, and even its substructures, around the oxygen-binding heme groups, making them more or less accessible to the environment. When oxygen binds to at least one of the heme groups (as happens in the oxygen-rich lungs), all of the heme groups become exposed to the environment and bind oxygen easily. The bond between oxygen and heme is a loose one, however, so that the oxygen can break free in the tissues, where the concentration of oxygen is relatively low, and thereby become available for use in the cells. When the last of the four heme subunits loses its oxygen, the structure of hemoglobin changes again, so that the size of the opening from the environment to the heme groups decreases, making it difficult for an oxygen molecule to rebind to the hemoglobin. In this way, hemoglobin stops itself from competing with the tissues for needed oxygen. When the red blood cell carrying hemoglobin returns to the lungs, where oxygen concentration is high, the cycle of oxygen binding, transport, and release starts again. Normally, iron binds with oxygen to form rust (iron oxide), but the structure of hemoglobin prevents this from happening, since it would inactivate the heme subunits. Carbon dioxide does not bind the heme in hemoglobin, but rather the amino groups at the ends of the hemoglobin's protein subunits. Hemoglobin transport is only one of a number of bodily mechanisms by which carbon dioxide travels from the tissues to the lungs for release to the air.