Showing posts with label hemoglobin. Show all posts
Showing posts with label hemoglobin. Show all posts

Monday, March 23, 2009

vampires rejoice

... at the prospect of unlimited supplies of human blood from the tap at their local:

British scientists to create 'synthetic' blood

But seriously, this was about time, as people are dying when blood reserves are running out, or getting too old, or lacking nitric oxide, or have been infected with some pathogen that nobody expected. This endeavour is a brilliant example of how cells from a single "leftover" embryo from IVF -- remember this is a clump of identical cells, which has never been inside a human being, and which would otherwise be thrown away -- can save hundreds of lives. According to the report in the Independent, cited above, we're three years away from clinical trials.

Tuesday, August 05, 2008

a plodding life

During my week off, I read Georgina Ferry's biography of Max Perutz, who solved the crystal structure of haemoglobin in an epic quest lasting over 3 decades, and who set up the Laboratory of Molecular Biology in Cambridge, which I understand has produced more Nobel laureates than France or Canada in the time since it opened.

All this makes for an exciting story, even though the protagonist is anything but a glittering star. Perutz was a very patient and persistent "plodder" who, while eager for success and recognition, was never seen as a genius and never had the over-sized ego that often comes with such a label. The persistent plodding won him the haemoglobin structure and the Nobel prize, while his modesty allowed him to quietly run a world-leading institute where he had to handle primadonnas like Francis Crick.

Obviously, the book is a must for anybody interested in proteins. For everybody else, I was worried a bit that it might turn out a bit boring as I knew that Max was a less than glittering person. But I think the author has managed the trick to turn his plodding life into a compelling story, which should be interesting for non-specialist readers as well. The main lesson for the general public is, of course, that one doesn't have to be a towering genius of stature of a Crick or Bernal in order to be a successful scientist. Relatively ordinary people can make an impact too.

Friday, April 25, 2008

blood transfusion risks

Many blood transfusions may increase risks, doctors warn, the Guardian reports, apparently based on a story in New Scientist. Well, I agree completely, but then the piece goes on rambling about how boffins don't understand why blood that has been stored is often doing more harm than good.

In fact, last October, two independent and very convincing papers (one was actually commissioned to check the findings of the other, because of the enormous importance of the issue!) showed that there is a very simple reason, and a very simple way to fix the problem.

Fresh blood contains nitric oxide (NO) bound to hemoglobin, which it loses within hours of storage. NO is needed as a signal to widen the blood vessels. So old blood without NO will lack the vessel-dilating effect and thus the oxygen provision may be no better than or even worse than what the patients could achieve with their own blood. The problem is easy to fix, as NO can be added to the stored blood before transfusion, making it good as new.

I reported all that in Chemistry World and in this blog entry, back in October. Naively, I would have hoped that by now medics would have made moves to implement the fix, rather than scratching their heads over a question that has already been answered.

Saturday, March 08, 2008

happy birthday myoglobin

I wasn't around yet, but I am told that 50 years ago today a paper by J.C.Kendrew et al. appeared in Nature describing the first ever crystal structure of a protein, which was of course myoglobin.

This was made possible by more than three decades of research by Max Perutz and others at the LMB in Cambridge. Perutz himself had his sights set on haemoglobin, which is larger and more difficult and took a few years longer.

Today, of course, there are tens of thousands of crystal structures of proteins in the protein data bank (which today lists 41,915 Xray structures of proteins and nucleic acids), and some papers contain structures of several proteins or of huge assembly systems, sometimes only attached as one of several ways of characterizing the system in question.

Oh well. What I find most remarkable in this story is that it took 36 years or so from Perutz's start to the first structure. Try explaining to your funding agency today, if you don't have final results after 2 years, that it may take another 34 years to get there.

Tuesday, October 09, 2007

fresh blood

Researchers have found that over-generous blood transfusions can do more harm than good. Ironically, the measure which is supposed to improve oxygen provision to the patient's organs, can have the opposite effect.

Now there is an explanation to this paradox. It appears that the oxygen transport depends on a signalling process by which the red blood cells help to widen the blood vessels, and this involves nitric oxide bound to hemoglobin. Donor blood for transfusion can be legally stored for 42 days, but the nitric oxide disappears within the first few hours of storage, so virtually all stored blood samples are deficient in that respect.

While this sounds quite scary, there is a silver lining in that the NO content can be restored.

Read my story here:

Blood transfusion risk explained