Pehr Victor Edman was born on April 14, 1916, in Stockholm, Sweden. He studied medicine at the Karolinska Institute near Stockholm and received his Bachelor of Medicine degree in 1938. His studies and research were interrupted by World War II, as he served in the medical corps of the Swedish army. After the war, he returned to Karolinska Institute, where he received a medical doctorate in 1946 for work on the purification and characterization of angiotensin from bovine blood.
Edman was more interested in research than in practicing medicine. He, therefore, studied biochemistry and organic chemistry, and received a fellowship which allowed him to join the Rockefeller Institute of Medical Research in Princeton, NJ, USA, from 1946 to 1947. It was at Princeton that Edman began to work on finding a chemical way to determine the amino acid sequence of proteins. The notion that proteins had a defined molecular weight and structure had only recently been accepted, and methods to determine said structure were instrumental in understanding a protein’s function.
Edmans approach involved the use of phenylisothiocyanate (PITC), which reacts with the N-terminal amino acid of the protein. The amino acid can then be released from the protein using acid hydrolysis and identified as its hydantoin derivative. Repeating the process allows the determination of the protein’s amino acid sequence. The Danish biochemist Kaj Ulrik Linderstrøm-Lang termed the method “Edman Degradation”. Due to the limited yield of the reactions, it can only sequence peptides of up to about 30–60 residues, although this problem can be avoided by breaking large proteins down into smaller peptides and sequencing them separately.
Edman’s research career focused almost exclusively on improving his sequencing method. He returned to Sweden as Associate Professor at the University of Lund in 1947, where he first published his approach. In 1957, Edman was appointed Inaugural John Holt Director of Research at St. Vincent’s School of Medical Research in Melbourne, Australia. He remained in Melbourne until 1972 and was granted Australian citizenship in 1965. In 1967, he developed an automated sequencer, the so-called “Sequenator”, together with his assistant Geoffrey Begg. The machine allowed the faster analysis of longer sequences. Edman insisted that the device would not be patented, and by 1973, over 100 sequencers based on his approach were in use worldwide. Today, they are in widespread use.
In 1972, Edman returned to Europe and was appointed Director of Protein Chemistry at the Max Planck Institute for Biochemistry in Martinsried near Munich, Germany. Pehr Victor Erdman died in Munich on March 19, 1977.
Pehr Victor Edman is the answer to Guess the Chemist (52).
Sources
- Edman, Pehr Victor (1916–1977),
F. J. Morgan,
Australian Dictionary of Biography 1996. - Pehr Victor Edman,
S. Miles Partridge, B. Blombäck,
Biogr. Mem. Fellows R. Soc. 1979.
DOI: 10.1098/rsbm.1979.0008 - Obituary Pehr Victor Edman,
S. Moore,
Trends Biochem. Sci. 1977, 2, N160.
DOI: 10.1016/0968-0004(77)90360-7
Selected Publications
- A Protein Sequenator,
P. Edman, G. Begg,
Eur. J. Biochem. 1967, 1, 80–91.
DOI: 10.1111/j.1432-1033.1967.tb00047.x - Human fibrinopeptides: isolation, characterization and structure,
B. Blombäck, M. Blombäck, P. Edman, B. Hessel,
Biochim. Biophys. Acta 1966, 115, 371–396.
DOI: 10.1016/0304-4165(66)90437-5 - Identification and Semiquantitative Determination of Phenyl Thiohydantoins.,
P. Edman, J. Sjöquist, K. Lunde, N. A. Eliasson, B. Thorell,
Acta Chem. Scand. 1956, 10, 1507–1509.
DOI: 10.3891/acta.chem.scand.10-1507 - Method for Determination of the Amino Acid Sequence in Peptides,
P. Edman, E. Högfeldt, L. G. Sillén, P.-O. Kinell,
Acta Chem. Scand. 1950, 4, 283–293.
DOI: 10.3891/acta.chem.scand.04-0283 - Preparation of Phenyl Thiohydantoins from Some Natural Amino Acids.,
P. Edman, E. Dynesen, M. Webb, M. Rottenberg,
Acta Chem. Scand. 1950, 4, 277–282.
DOI: 10.3891/acta.chem.scand.04-0277
Also of Interest
- 100th Birthday: Christian B. Anfinsen,
ChemViews Mag. 2016.
Distinguished biochemist explored important aspects of protein folding - 50th Guess the Chemist,
ChemViews Mag. 2016.
DOI: 10.1002/chemv.201600009
