Makio murayamas biography

That was Ingram and Hunt. Williams: Hunt, right. Who were your collaborators in the laboratory that you were working with? Murayama: Well, I was at Cal Tech on my own. That was -- I received a postdoctoral fellowship under Linus Pauling. And this is the year that Linus Pauling received his Nobel Prize. I got there in July, and a couple of months later he got a phone call from Stockholm, and, well, we had no idea what a great deal of excitement and joy that was.

I think it was he meant to be a joke or something, you know. The alpha helix was one of the many things. But, anyway, I was working on what is known as the sulfhydryl group. This was the method of determination was electrochemistry, amperometric titration, which was not very popular. I ended up getting a patent on that. This took place before I got to Cal Tech.

And so while I was in Cal Tech, I built the gadget and cranked out data on it, and the thing to do was to change the temperature, raise the temperature, and the number of titratable sulfhydryl group increased. Reduce the temperature down to zero, and it decreased in half, when 50 percent was titratable, indicating that some sort of architectural change took place and that 50 percent of the sulfhydryl groups got muzzled, became unavailable to the ion.

Mercaptan [sp. After you titrate mercaptan [sp. So, in the course of amperometric titration at zero degrees and at 38 degrees, I discovered the negative temperature caused the titration of S hemoglobin. You were still a postdoc at this time? So your research at Cal Tech was this titration, amperometric titration of sulfhydryl groups.

Is that correct? Murayama: The physical chemistry of S hemoglobin, the main thing. And amperometric titration was one aspect of the physical chemistry investigation into sickle cell hemoglobin. And what happens is that the sickle cell hemolysate gels upon deoxygenation warmed up in my hand. I was holding the test tube actually like this, and the only thing I had was a beaker full of ice chips.

And I put in an ice chip and then shake, and, lo and behold, turned into liquid. Murayama: I must be out of my mind. I discovered something. And I started to, well, this is quite contrary to what you expect. If I wanted to make jello so jello will set, I put the ice back. Murayama: Well, you know, this is it; I did a lot of searching in the laboratory, in the library.

Williams: This is the one in Nature. So, the JBC paper I guess is where you first reported it. I suppose it was confirmed by this optical dispersion. This was a tremendous excitement. I was starting an experiment. This was done in Building 4 basement. There was a gadget there that occupied a whole room in those days. I suppose I did a lot of thinking, and there are lots of smart guys around, you know.

Murayama: [? You were doing these experiments. Murayama: Like everything else, I do everything alone. I had to find these people for the blood specimen. It was fun. Murayama: You know the difference is so bizarre. Williams: And how many times did you do it over? I mean, obviously, the first time you did it, you probably thought maybe I did something wrong.

Murayama: Just like the first time, it could be the wrong time, but the second time around Williams: Trial and error. So you have this exciting conclusion. Perhaps you can tell me. I know that you did a lot of this work by yourself, but you were speaking with Pauling about this. Were there any other people that you worked with or, maybe not collaborators, but I guess colleagues?

Murayama: Yeah. Well, most of the work done at NIH, people, nobody was interested in sickle cell hemoglobin in those days. Nothing has been done. There are a lot of other fine refinements. What I do is muzzle the binding site, hydrophobic binding site, with a bit of urea. The patient stays out of the hospital. I never said that this is a cure. This is to extend the survival time.

Description written by:. Return to Archive. About Us. Privacy Policy. Terms of Use. NIH scientist Makio Murayama with the molecular model of hemoglobin that he built to study SCD and explain why red blood cells take on a sickle shape. In his NIH oral history , Murayama expressed his penchant for working alone, his solitary endeavors perhaps analogous to the paucity of research devoted to understanding SCD at that time.

Down the road, the work would ultimately pay dividends, and his conclusions about hemoglobin dynamics would inform the first drugs used to treat the disease PMID: Science has since steamed ahead, and for the , people in the United States and 8 million people worldwide with SCD, there are now two big reasons to be optimistic. But they do represent a future in which a cure is available to more people.

Makio murayamas biography

The discovery in several laboratories that sickle hemoglobin formed long fibers inside red blood cells, which impaired circulation and drove disease manifestations, renewed interest among a handful of NIH investigators in biophysical studies that would eventually lead to treatments. Illustration of sickle red blood cells and normal red blood cells.

The misshapen cells occlude circulation and can result in disease manifestations including sudden pain crises, chronic pain, organ damage, and anemia. Approved drugs were still decades away. Schechter and colleagues focused on using new methods at that time, such as nuclear magnetic resonance, to understand the thermodynamics of how sickle hemoglobin molecules aggregate or polymerize inside deoxygenated red blood cells.

Learn about our Editorial Policies. T oday, the cause of sickle cell disease is well understood to be a point mutation in a hemoglobin gene called HBB that makes red blood cells grow stiff and misshapen. Sixty years ago, however, top scientific minds struggled to understand the mechanisms of that so-called sickling of cells. The answer came, in part, thanks to a massive physical model of the protein deoxyhemoglobin hemoglobin not yet bonded to oxygen that was meticulously assembled over six years by Japanese-American chemist Makio Murayama.