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Hemoglobin in sentence

37 examples of Hemoglobin in a sentence

But she did find heme, which is the biological foundation of hemoglobin.
And those red molecules are hemoglobin.
And hemoglobin acts as a molecular sponge to soak up the oxygen in your lungs and then carry it to other parts of the body.
A toxic gas called carbon monoxide crosses that membrane into the blood, binding to hemoglobin and displacing the oxygen it would usually have transported around the body.
Millions suffer from sickle cell anemia because they have a single A to T point mutations in both copies of their hemoglobin gene.
So cutting this already-mutated hemoglobin gene that causes sickle cell anemia won't restore the ability of patients to make healthy red blood cells.
To perform this vital task, red blood cells are filled with hemoglobin proteins to carry oxygen molecules.
But in sickle cell disease, a single genetic mutation alters the structure of hemoglobin.
Rods of hemoglobin cause the cell to deform into a long, pointed sickle.
And if a child inherits a copy of the mutation from only one parent, there will be just enough abnormal hemoglobin to make life difficult for the malaria parasite, while most of their red blood cells retain their normal shape and function.
But promising new medications are intervening in novel ways, like keeping oxygen bonded to hemoglobin to prevent sickling, or reducing the stickiness of sickled cells.
And the ability to edit DNA has raised the possibility of enabling stem cells to produce normal hemoglobin.
When you inhale, your lungs transfer oxygen into hemoglobin molecules, and the pulse oximeter measures the ratio of oxygenated to oxygen-free hemoglobin.
When the LED shines into your finger, oxygen-free hemoglobin in your blood vessels absorbs the red light more strongly than its oxygenated counterpart.
So the amount of light that makes it out the other side depends on the concentration ratio of the two types of hemoglobin.
All molecules, including hemoglobin, absorb light at different efficiencies across this spectrum.
For example, hemoglobin has a shape in the lungs perfectly suited for binding a molecule of oxygen.
When hemoglobin moves to your muscle, the shape changes slightly and the oxygen comes out.
There's actually a company in Greece that produces these cigarettes that actually contain hemoglobin from pigs in the filter.
A second major advance came a few months later, when Max Perutz discovered a technique to determine the structures of large molecules like myoglobin and hemoglobin.
The next year, he was given excellent hemoglobin crystals and soon produced the best X-ray diffraction patterns to date.
In the early twentieth century, researchers began to examine hemoglobin – the protein responsible for carrying oxygen from the respiratory organs to the rest of the body – in red blood cells.
They found that, when isolated from aging cells – whether from human or cow blood, or from genetically engineered sources – free hemoglobin can be rejuvenated, chemically stabilized, and re-infused as a blood “substitute” that can carry oxygen as effectively as red blood cells, but for a much shorter time.
But free hemoglobin can wreak havoc in the human body, causing hypertension, cardiac arrest, or even death.
Indeed, in almost all living creatures, hemoglobin is encapsulated in red blood cells, which protect the body from the protein’s negative effects (and, in turn, protect hemoglobin from the body’s digestive enzymes).
Outside of red blood cells, “good” ferrous iron – the only oxygen-carrying form – is oxidized uncontrollably to form the “bad” ferric and “ugly” ferryl forms of hemoglobin.
When released into a person’s circulatory system, hemoglobin in these higher oxidation states eventually self-destructs, damaging molecules in surrounding tissue.
Given that these mischievous forms of hemoglobin are difficult to study in living systems, researchers have largely ignored them.
Instead, they have focused on strategies for preventing the kidneys from filtering the infused hemoglobin; the hemoglobin from leaking through the blood-vessel walls; and synthetic hemoglobin from destroying nitric oxide (a gas produced in blood vessels that helps them to dilate and increase blood flow).
Researchers (including at my laboratory) have investigated how the body naturally handles the occasional release of hemoglobin from aging red blood cells and from cells affected by blood diseases, such as hemolytic anemia.