Richard Synge Biography

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World of Chemistry on Richard Synge

Richard Synge made important contributions in the fields of physical chemistry and biochemistry. He is best known for the development of partition chromatography, a collaborative effort undertaken with A. J. P. Martin in the late 1930s and early 1940s. As a result of their work, Synge and Martin received the 1952 Nobel Prize in chemistry.

Richard Laurence Millington Synge was born on October 28, 1914, in Liverpool, England, to Laurence Millington Synge, a stockbroker, and Katherine Charlotte (Swan) Synge. He was the oldest of three children and the only son. After growing up in the Cheshire area of England, he attended Winchester College, a private preparatory school, where he won a classics scholarship to attend Trinity College at Cambridge University. After listening to a speech given by the noted biochemist Frederick Gowland Hopkins, however, he decided to forego his education in the classics and instead pursue a degree in biochemistry at Trinity.

Synge undertook graduate studies at the Cambridge Biochemical Laboratory in 1936, receiving his Ph.D. in 1941. His doctoral research concerned the separation of acetyl amino acids. It was at this time that Synge first met Archer Martin, who was engaged in building a mechanism for extracting vitamin E. They began to work together on a separation process, which was delayed when Martin left for a position at the Wool Industries Research Laboratories in Leeds, England. Synge was able to join Martin there in 1939, when he received a scholarship from the International Wool Secretariat for his work on amino acids in wool.

Synge and Martin's work built on the adsorption chromatography techniques first developed by Mikhail Tswett, a Russian botanist, who evolved the procedure in his work on plant colors. Like Tswett, Synge and Martin's goal was to separate the various molecules that make up a complex substance so that the constituent molecules could be further studied. In order to achieve this goal, Tswett had filled a glass tube with powder, then placed a sample of the complex material to be studied at the top of the tube. When a solvent was trickled into the tube, it carried the complex material down into the powder. As the solution moved through the tube, the molecules of the different substances would separate and move at different speeds depending on their chemical attraction to the powder. While Tswett's technique was useful, it did not have universal application; there were a limited number of materials that could be used for the powder filling, and therefore only a limited number of substances could be identified in this manner.

In addition to Tswett's adsorption chromatography, there also existed the process of countercurrent solvent extraction. This technique involves a solution of two liquids that do not mix, such as alcohol and water. When a complex substance is applied to this solution, the molecules separate depending on whether they are more attracted to the water or the alcohol. Synge and Martin's breakthrough involved the combination of adsorption chromatography and countercurrent solvent extraction. This was achieved by using a solid substance adsorbent such as fine cellulose paper in place of Tswett's powder. In one application of the procedure, a complex mixture of molecules is spotted on one end of the paper, then that end is placed in a solution that might contain alcohol and water or chloroform and water. As the liquids flow through the paper, transporting the complex substance, the molecules in the substance separate depending both on their rate of adsorption by the paper and also by their affinity for either of the two liquids. When the process is completed, a series of spots is visible on the strip of paper. Each spot depicts one type of molecule present in the complex substance.

Synge and Martin had made early progress on partition chromatography during their time at Cambridge, but the need by industry and medicine for a more reliable technique spurred further research. At Leeds, they built a forty-unit extraction machine and experimented with various solvents and filtering materials. Their collaboration continued after Synge left to become a biochemist at the Lister Institute of Preventive Medicine in London in 1943, and by 1944 the improved cellulose filter method resulted. Later, they developed a two-dimensional chromatography process wherein two solvents flow at right angles to one another. This technique yielded an even sharper degree of molecular separation.

Partition chromatography was readily adopted by researchers for a variety of biochemical separations, especially those involving amino acids and proteins. Using the process in his doctoral research, Synge was able to separate and analyze the twenty amino acids found in protein. The technique was used in studies of enzyme action as well as in analyses of carbohydrates, lipids, and nucleic acids. Partition chromatography also became a useful tool for the food, drug, and chemical industries. Further experimentation with the process allowed proteins to be identified through the use of radioactive markers. The result of this marking was the ability to produce a photograph of the biochemical separation. The marking technique was used extensively by other biochemists, notably Melvin Calvin for his work in plant photosynthesis, and Walter Gilbert and Frederick Sanger for their research into DNA sequencing. All three would later receive the Nobel Prize for discoveries made using partition chromatography .

Continuing his research of amino acids and peptides, Synge traveled to the Institute of Biochemistry at the University of Uppsala, Sweden, in 1946. There, he and Arne Tiselius, the Swedish biochemist, studied other separation methods, especially electrophoresis and adsorption. Back home, Synge applied this knowledge toward the isolation of amino acids in rye grass in order to study their structure, a subject he collaborated on with J. C.Wood. He also used the new techniques to study the molecular makeup of plant juices, examining the juices' role as a stimulator in bacteria growth. Partition chromatography was an important factor in other research carried on by Synge at that time. With D. L. Mould, he separated sugars through electrokinetic ultrafiltration in order to study the metabolic process. With Mary Youngson, he studied rye grass proteins. He and E. P. White were able to isolate a toxin called sporidesmin, which produces eczema in sheep and other cud-chewing animals. Synge's findings in all of these areas benefited efforts by agriculture, industry, and medicine to improve human health and well-being.

In 1948 Synge accepted a position as director of the Department of Protein Chemistry at Rowett Research Institute in Scotland. From 1967 until his retirement in 1976, he was a biochemist with the Food Research Institute in Norwich. He closed out his academic career as an honorary professor in the School of Biological Sciences at the University of East Anglia from 1968 until 1984. In addition to the Nobel Prize, Synge received the John Price Wetherill Medal of the Franklin Institute in 1959. He held memberships in the Royal Society, the Royal Irish Academy, the American Society of Biological Chemists, and the Phytochemical Society of Europe. He married Ann Stephen, a physician and the niece of writer Virginia Woolf, in 1943. They had seven children. Synge died on August 18, 1994, of myelodysplastic syndrome.