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The beginnings of Mass Blood Donations

  • 13-03-2015 2:27am
    #1
    _Tombstone_
    Closed Accounts Posts: 3,006 ✭✭✭


    http://blog.longreads.com/2015/03/10/a-very-naughty-little-girl/

    They're not messing about the long read^^.

    This is the story of Janet Vaughan who started what is now the National Blood Service in the UK in the lead up to the German Bombing in the 1940s.

    Tis a good ould read, type of bottle blood_transfusion_bottle_capped_with_associated_parts_eng_wellcome_l0066184.jpg?w=300&h=452 type of chair, sodium citrate, where to store it so it didn't get blown up, how to move it.

    It's the beginnings of a system we don't even notice and without which how many would die?


    And now look at how complex it has got trying to provide for rare blood types around the world.


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  • #2
    _Tombstone_
    Closed Accounts Posts: 3,006 ✭✭✭_Tombstone_


    Transforming all donated blood into a universal type
    What do you do when a patient needs a blood transfusion but you don't have their blood type in the blood bank? It's a problem that scientists have been trying to solve for years but haven't been able to find an economic solution - until now.

    University of British Columbia chemists and scientists in the Centre for Blood Research have created an enzyme that could potentially solve this problem. The enzyme works by snipping off the sugars, also known as antigens, found in Type A and Type B blood, making it more like Type O. Type O blood is known as the universal donor and can be given to patients of all blood types.

    "We produced a mutant enzyme that is very efficient at cutting off the sugars in A and B blood, and is much more proficient at removing the subtypes of the A-antigen that the parent enzyme struggles with," said David Kwan, the lead author of the study and a postdoctoral fellow in the Department of Chemistry.

    To create this high-powered enzyme capable of snipping off sugars, researchers used a new technology called directed evolution that involves inserting mutations into the gene that codes for the enzyme, and selecting mutants that are more effective at cutting the antigens. In just five generations, the enzyme became 170 times more effective.

    With this enzyme, UBC associate professor Jayachandran Kizhakkedathu and colleagues in the Centre for Blood Research were able to remove the wide majority of the antigens in Type A and B blood. But before it can be used in clinical settings, the enzyme used would need to remove all of the antigens. The immune system is highly sensitive to blood groups and even small amounts of residual antigens could trigger an immune response.


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