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Scientists think that they’ve found the key to creating universal blood -- and hairy best friend gay sex videoit’s in your poop.

At a press conference held by the American Chemical Society earlier this week, a team of chemists lead by Steve Withers from the University of British Columbia announced that they were able to identify an enzyme -- found in gut bacteria -- that can make universal Type-O blood from other blood types.

SEE ALSO: We may have a new weapon to fight dangerous superbugs (and we're gonna need it)

What they’ve done is collected samples of this bacteria from human feces, let them cultivate the enzyme in a lab, and then applied the enzyme to Type A blood.

If all goes according to plan in the lab, that enzyme converts the Type A blood into O.

“The idea is that if you are able to cut the A and B sugars off of the red blood cells, you could transform it to the O blood cell,” Withers said in an interview.

Effectively, the team may have found a way to solve the blood shortage crisis that affects hospitals around the world.

A nurse carries vials Credit: Getty Images

So, exactly how does this work?

There are four principle blood types, with two subcategories -- bringing the total number of possible blood types to eight.

Type A, B, and O blood all share the same core red blood cell structure. However, Type A and B both have additional unique antigens made up of complex sugars attached to the outside of the blood cell that makes them incompatible with other blood types.

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The lack of those additional sugars is what makes Type O universal, because it’s able to mix with all other blood types.

Scientists have long thought that removing the antigens was the way to go when trying to create a universal blood type.

Back in the early 1990s, a study came out showing that a different enzyme could be used for this kind of application.

“But the process was not efficient enough. It took way too many enzymes and they were not successful with the A blood type at all,” Withers explained.

The newly-discovered enzyme is 30 times more efficient than all others found on previous attempts.

“What that means in practical terms is we need to use 30 times less than you need of the other enzyme,” Withers said.

A woman donates blood to help hospital meet the high blood transfusion demands after a bad outbreak of E.Coli in Europe. Credit: Getty Images

“And the other factor that’s a little less obvious is that it’s super important that we remove all traces of that added enzyme before it’s put into a human because of the dangers of immune responses to bacterial enzymes. So the less enzymes we have to use, the less material we have to remove.”

Dana Devine, a scientist at the Center for Blood Research unaffiliated with the study, said that may seem like a small difference but it was the efficiency that kept all previous attempts from being successful.

“He’s potentially figured out how to make this process more effective using less enzymes and faster which would make it cheaper. Researchers in the early 2000s were doing this but it required a larger quantity of enzymes and was likely nixed because of how expensive it was,” Devine said of Withers' work.

This new development could be the difference between life and death.

When the situation is dire and medical personnel do not have the time to determine a patient’s blood type, they defer to Type O since it can be universally applied.

So if this enzyme is able to make Type O overnight, the blood shortage crisis around the world could be a thing of the past.

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