Hans Lineweaver

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Hans Lineweaver
Born(1907-12-25)December 25, 1907
Pickens, West Virginia[1]
DiedJune 10, 2009(2009-06-10) (aged 101)
Walnut Creek, California[1]
EducationGeorge Washington University (BA, 1933), Johns Hopkins University (PhD 1936)
Known forDouble-reciprocal plot
Children11 great-greatgrandchildren at the time of his death[1]
Scientific career
FieldsBiochemistry
InstitutionsU.S. Department of Agriculture, Western Regional Research Center, Albany, California

Hans Lineweaver (December 25, 1907 – June 10, 2009) was an American physical chemist, who is credited with introducing the double-reciprocal plot or Lineweaver–Burk plot.[2] The paper containing the equation was co-authored by Dean Burk, and was entitled "The Determination of Enzyme Dissociation Constants (1934)". It remains the most frequently cited paper[3] to appear in the Journal of the American Chemical Society.[4] Lineweaver and Burk collaborated with the eminent statistician W. Edwards Deming on the statistical analysis of their data:[5] they used the plot for illustrating the results, not for the analysis itself.

Linearizations of the Henri-Michaelis-Menten law of enzyme kinetics [6][7] were important in the era before general availability of computers to determine the parameters Vmax and Km from experimental data, even though there are significant statistical problems involved in this procedure.[8][9] These are still used for data presentation. All three possible methods of linearization (now often called Lineweaver-Burk, Eadie-Hofstee and Hanes plots, respectively) were originally proposed by Barnet Woolf, who was unable to formally publish them due to injuries received in a car accident. However, he had discussed them with his close friend and fellow member of the British Communist Party, J. B. S. Haldane, who referred to them in his seminal book on enzyme kinetics.[10] However, the linearizations were largely ignored until they were re-invented by the authors whose name they now bear.[11]

Lineweaver developed the Lineweaver–Burk equation in 1934 while still a graduate student, working as a laboratory assistant under Burk at the U.S. Department of Agriculture in Washington, D.C. He was an internationally recognized authority on food technology as applied to the processing, preservation and safety of poultry and eggs.

Early life[edit]

Lineweaver received his Bachelor of Arts degree in chemistry from George Washington University in 1930, and continued on to receive his Master of Arts degree there in 1933. He obtained his PhD in physical chemistry from Johns Hopkins University in 1936. In 1929, a year before graduating, he was appointed a junior scientific aide to the U.S. Department of Agriculture, and worked as a chemist in the fertilizer section of the Bureau of Chemistry and Soils. In 1930, Lineweaver was transferred to the Food Research Division of the USDA as an associate chemist, pursuing enzyme research. In 1939, he was transferred to the newly built Western Regional Research Laboratory of the USDA in Albany, California, as senior biochemist and head of the enzyme section in the biochemical division. During and after World War II, Lineweaver collaborated with the Quartermasters Corps of the Armed Services in enzyme work related to poultry and powdered egg flavor and processing. In 1948, he was appointed chief of the WRRL Poultry Laboratory in 1949, a position he held until his retirement in 1973, after 44 years of continuous service for the U.S. Department of Agriculture.

During his career, Lineweaver was the author or co-author of nearly 100 technical publications and six patents, over half of which concern aspects of poultry and eggs, such as effects of processing on tenderness,[12] and the remainder with enzymology or other aspects of biochemistry, including, for example, a review of pectic enzymes.[13] He and his team developed the first USDA-approved method of pasteurizing egg white, and established a process of converting waste feathers into feed. He has received honors, citations and awards, including the Nicholas Appert Award from the Institute of food Technologists (IFT) in 1973. Hans was a President of the IFT in 1971, and was appointed by the State Department to chair the U.S. Delegation to the 12th World Poultry Congress in Australia in 1962. He was an active member or chairman of organizations including the American Chemical Society, the Poultry Science Association, the World Poultry Science Association, the Poultry and Egg National Board, the Institute of American Poultry Industries, and the American Society of Biological Chemists.

Personal life[edit]

Hans Lineweaver was born in Pickens, West Virginia, on Christmas Day, 1907, the second child of Rev. Dr. Jesse Luther and Lucille Lineweaver. He was married in 1936 to Margaret Peggy Coon of Baltimore, MD, and was the father of 2, the grandfather of 15, the great-grandfather of 29 at the time of his death, and the great-great grandfather of 11. He lived in retirement in Walnut Creek, California. Lineweaver died in Walnut Creek on June 10, 2009, at age 101.[1]

References[edit]

  1. ^ a b c d Cornish-Bowden, Athel (2012). Fundamentals of Enzyme Kinetics (4th ed.). Wiley-Blackwell, Weinheim. pp. 25–75. ISBN 978-3-527-33074-4.
  2. ^ The credit is misleading, as all three linearizations of the Michaelis–Menten equation were proposed by Barnet Woolf and first published by J. B. S. Haldane: see below.
  3. ^ Almost 14000 citations by March 2023.
  4. ^ Lineweaver, H; Burk, D. (1934). "The Determination of Enzyme Dissociation Constants". Journal of the American Chemical Society. 56 (3): 658–666. doi:10.1021/ja01318a036.
  5. ^ Lineweaver H, Burk D, Deming, W E (1934). "The dissociation constant of nitrogen-nitrogenase in Azobacter". Journal of the American Chemical Society. 56: 225–230. doi:10.1021/ja01316a071.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Henri, Victor (1902). "Theorie generale de l'action de quelques diastases". Compt. Rend. Acad. Sci. Paris. 135: 916–919.
  7. ^ Michaelis, L.; Menten, M.L. (1913). "Die Kinetik der Invertin-Wirkung". Biochem. Z. 49: 333–369.
  8. ^ Wilkinson, G.N. (1961). "Statistical estimation in enzyme kinetics". Biochem. J. 80 (2): 324–332. doi:10.1042/bj0800324. PMC 1244002. PMID 13785321.
  9. ^ Johansen G, Lowry R (1961). "Statistical analysis of enzymic steady-state rate data". Comptes rendus des travaux du Laboratoire Carlsberg. 32: 185–214. PMID 14451942.
  10. ^ Haldane, J.B.S.; Stern, K.G. (1932). Allgemeine Chemie der Enzyme. Dresden: Steinkopf.
  11. ^ Haldane, J.B.S (1957). "Graphical methods in enzyme chemistry". Nature. 179 (4564): 832. Bibcode:1957Natur.179R.832H. doi:10.1038/179832b0. S2CID 4162570.
  12. ^ Klose, A A; Pool, M F; Wiele, M B; Hanson, H L; Lineweaver, H (1959). "Poultry tenderness 1. Influence of processing on tenderness of turkeys". Food Technology. 13 (1): 20–24.
  13. ^ Lineweaver, H; Jansen, E F (1951). "Pectic Enzymes". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 11. pp. 267–295. doi:10.1002/9780470122563.ch5. ISBN 9780470122563. PMID 24540593. {{cite book}}: |journal= ignored (help)
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