Dakin, Henry Drysdale
DAKIN, HENRY DRYSDALE
(b. London, England, 12 March 1880; d. Scarborough-on-Hudson, New York, 10 February 1952)
The youngest of eight children of Thomas Burns Dakin and Sophia Stevens, Dakin grew up in Leeds, where his father owned an iron and steel business. After finishing public school, he apprenticed with the Leeds city analyst, for whom he tested sulfur content at gasworks. Dakin subsequently obtained a B.Sc. (1901) from Yorkshire College, Leeds (then part of Victoria University, Manchester, now the University of Leeds), Dakin also received the D.Sc. from Leeds in 1907. At Leeds, Dakin worked extensively with Julius B. Cohen, an organic chemist who was investigating the optical activity of biological compounds, a topic that figured in Dakin’s later work. He remained as an unofficial demonstrator in Cohen’s laboratory for a year after graduation and in 1902 was awarded an 1851 Exhibition Prize, which enabled him to do research at the Lister Institute in London and to spend time at Karl Kossel’s laboratory in Heidelberg.
In 1905 Dakin accepted an invitation to join the private laboratory of Christian A. Herter in New York City, of which he became director upon Herter’s death in 1910. In July 1916 he married Herter’s widow, Susan Dows Herter, and two years later they moved to Scarborough-on-Hudson, where he reestablished the laboratory. Dakin never held an academic appointment but was in regular contact with the research community through frequent trips to England and through his service, from 1910 to 1930, as one of four editors of the Journal of Biological Chemistry. (The journal had been founded by Herter.) Later in life Dakin was science adviser to the Merck Institute of Therapeutic Research and a director of Merck and Company.
Dakin received numerous honors, including honorary degrees from Yale University (1918), the University of Leeds (1936), and the University of Heidelberg (1938); the French Legion of Honor; and the Conné Medal of the New York Chemists Club. He was elected a fellow of the Royal Society in 1917, He suffered from extreme shyness and thus did not attend public meetings or conferences; he is not known ever to have given a lecture. Dakin therefore declined an invitation to give the Croonian Lecture;and when he was awarded the Davy Medal in 1941, it was presented privately by Henry Dale in Dakin’s library.
Dakin’s early work focused on enzymes, beginning with a study, done while still a student of Cohen’s, on the mode of action of lipase. While at Heidelberg he and Kossel discovered arginase, and at the Lister Institute he examined the action of esterases on the esters of mandelic acid. His discovery of the stereochemical specificity of these enzymes led him to propose that the first step in hydrolysis consists in the ester’s combination with the enzyme.
When he went to Herter’s laboratory Dakin focused on the intermediary (β) metabolism of amino acids and fatty acids. As an oxidizing agent he employed a solution of hydrogen peroxide with a trace of ferrous sulfate. With this oxidation technique Dakin provided confirming evidence for Knoop’s demonstration of β oxidation of fatty acids when he showed that those fatty acids with an odd number of carbon atoms produced phenylacetic acid, while those with an even number yielded benzoic acid. Dakin continued this research in an attempt to identify the various intermediaries of fatty acid oxidation and proposed an account in which the fatty acids are oxidized at the β carbon, generating ketone bodies as intermediates. Dakin hypothesized that successive β oxidations continued until one molecule of acetoacetic acid remained. This account of the intermediate steps in fatty acid oxidation was widely accepted until the 1940’s.
After taking over Herter’s laboratory, Dakin frequently worked alone. A significant exception was his collaboration with Harold W. Dudley. One of their major investigations resulted in the discovery and characterization of glyoxalase, an enzyme that converts glyoxals into corresponding acids. Another joint endeavor concerned the effect of alkali on the properties of proteins. Dakin’s interest in this stemmed from his observation, made while working with Kossel, of the effect of alkalies on the optically active hydantoins. He ascribed this change in optical activity to tautomeric change and hypothesized that similar effects should be observed in the polypeptide chains of proteins.
With Dudley, Dakin undertook a study of the amino acids produced from casein treated with alkali that demonstrated that the interior amino acids, but not the terminal ones, were racemized. Thus the position in the protein affected whether the amino acid was racemized. In a later extension of this work, Dakin and Henry Dale showed that crystalline albumins from hen and duck eggs, although very similar in their quantitative composition, behave as distinct antigens in anaphylactic reactions and, upon alkali treatment, yield amino acids with different optical activity (as a result of different sequencing of the amino acids).
During the early part of World War I, Dakin worked in a hospital at Compiègne. France, and there developed a buffered hypochlorite solution for treatment of infected wounds that was named for him. Later in the war he made several trips to the Lister Institute, where the research departments of the Medical Research Committee were housed, and, under its auspices, issued numerous publications (including, with Edward K. Dunham, A Handbook on Antiseptics) on disinfecting and sterilizing wounds.
After the war Dakin worked on developing techniques for isolating amino acids from proteins and studied the oxidative catabolism of fatty acids, unsaturated acids, hydroxyacids, and amino acids by animal tissues and yeast. The last major project he undertook was an investigation begun in the 1930’s of the hematopoietic factor in liver. Although he failed to isolate the factor, he and Randolph West developed a method for producing the factor in a purer state than was previously available. This made possible the commercial production of the hematopoietic factor that could be used intravenously with safety in the treatment of pernicious anemia.
In addition to Dakin’s original contributions to biochemical research, he wrote two highly influential reviews, Oxidations and Reductions in the Animal Body surveyed the already vast literature on biological oxidations up to 1912, and “Physiological Oxidations” provided an update to 1920.
I. Original Works. Dakin’s major writings include “The Oxidation of Amino Acids with the Production of Substances of Biological Importance,” in Journal of Biological Chemistry, 1 (1906), 171–176; Oxidations and Reductions in the Animal Body (London and New York, 1912: 2nd ed., 1922); “Studies on the Intermediary Metabolism of Amino Acids,” in Journal of Biological Chemistry, 14 (1913), 321–333; “On Glyoxalase,” ibid., 423–431, written with Harold W. Dudley; “The Racemization of Proteins and Their Deriatives Resulting from Tautomeric Change. Part II. The Racemization of Casein,” ibid., 15 (1913), 263–276, written with Dudley; “On the Use of Certain Antiseptic Substances on the Treatment of Infected Wounds,” in British Medical Journal (1915), 2 , 318; A Handbook on Antiseptics (New York, 1917), written with Edward K. Dunham: “Chemical Structure and Antigenic Specificity, A Comparison of the Crystalline Egg-Albumins of the Hen and the Duck,” in Biochemical Journal, 13 (1919), 248–257, written with Henry H. Date; “Physiological Oxidations,” in Physiological Reviews, 1 (1921), 394–419; and “Observations on the Chemical Nature of a Haematopoietic Substance Occurring in Liver,” in Journal of Biological Chemistry. 109 (1935), 489–522. written with Randolph West.
II. Secondary Literature. Obituaries of Dakin are H. T. Clarke “Henry Drysdale Dakin: 1880–1952,” in Journal of Biological Chemistry, 198 (1952), 491–494; and Percival Hartley. “Henry Drysdale Dakin,” in Obituaries of the Royal Society, 8 (1952), 129–148.