Hans Lineweaver

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.

  1. ^ a b c Cite error: The named reference fek was invoked but never defined (see the help page).
  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.