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Topic: Leonor Michaelis


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In the News (Thu 18 Jul 19)

  
  Leonor Michaelis (www.whonamedit.com)
From 1906 to 1922 Michaelis was head of the bacteriological department at the Urban hospital, becoming professor extraordinary 1908.
From 1922 to 1926 Michaelis was professor of biochemistry at the University of Nagoya, Japan, and 1926-1929 resident lecturer in medical research at the Johns Hopkins University in Baltimore.
Michaelis developed the equation with Menten to explain the relationship of the concentration of reactants on enzyme catalysed reactions.
www.whonamedit.com /doctor.cfm/2090.html   (392 words)

  
 Leonor Michaelis - Wikipedia, the free encyclopedia
Leonor Michaelis (January 16, 1875 – October 8, 1947) was a German biochemist and physician famous for his work with Maud Menten in enzyme kinetics and Michaelis-Menten kinetics.
Born in Berlin (Germany), he studied medicine in Freiburg, where he graduated in 1897.
Michaelis worked as assistant to Paul Ehrlich (1898–1899), Moritz Litten (1899–1902) and Ernst Victor von Leyden (1902–1906).
en.wikipedia.org /wiki/Leonor_Michaelis   (233 words)

  
 Women in Chemistry: Maud Menten
Michaelis was an M.D. similarly interested in doing fundamental research on the chemistry of the body’s processes, particularly on enzymes, or molecules in the body that spur other molecules into action.
When Michaelis and Menten started to work, it was already known that each enzyme in our bodies acts on a very specific chemical compound (substrate) to change it into something else—“like a key in a lock” said chemist Emil Fischer.
Michaelis and Menten were able to demonstrate that each enzyme, given enough substrate, has its own rate of causing that substrate to undergo chemical change.
www.chemheritage.org /women_chemistry/body/menten.html   (546 words)

  
 Maud Menten - Wikpedia   (Site not responding. Last check: 2007-09-17)
For her thesis work she had to go to the University of Chicago, as at that time women were not allowed to do research in Canada.
In 1912 she moved to Berlin where she worked with Leonor Michaelis, obtaining a Ph.D. in 1916.
Her most famous work was on enzyme kinetics together with Michaelis, based on earlier findings of Victor Henri.
www.bostoncoop.net /~tpryor/wiki/index.php?title=Maud_Menten   (242 words)

  
 Enzymes
Leonor Michaelis (1913) interpreted this effect to mean that ES complexes are formed until substrate saturation occurs and the increasing velocity ultimately reaches a plateau or maximum.
In their model, the rate of catalysis (V) increases with increasing [S], where V is defined as the number of moles of product formed per second.
Km is the Michaelis constant and can be defined as the substrate concentration at which the reaction rate is half of its maximal value.
neurobio.mcphu.edu /GalloWeb/Loudon_enzymes.htm   (2945 words)

  
 Nat' Academies Press, Biographical Memoirs V.67 (1995)
There he assimilated Michaelis's concept that the oxidation of organic compounds occurs in single electron steps (semiquinones) and later published a landmark paper with James LuValle that laid the foundation for what are now known as free radical reactions in biology.
Michaelis was not interested in the Neurospora work that Goddard had done, but he was excited when Goddard showed him that keratin (hair, wool, feathers), which is not normally digested by proteolytic enzymes, could be so digested if the disulfide bonds were first reduced.
He and Michaelis showed that the fibrous structure of the protein could be degraded by reduction of the disulfide bonds:
www.nap.edu /openbook/0309052386/html/183.html   (422 words)

  
 Michaelis and Menten
Leonor Michaelis (1875-1940) and Maud Leonora Menten (1879-1960)
That it is so appears from all earlier investigations, and especially it was shown by L. Michaelis and H. Davidson...
The function left undetermined on the right-hand side of this equation is given a definite form by means of our equation (8), otherwise nothing is altered and one sees forthwith by comparison of (8) and (10) that the constant of equation (8) must be proportional to the ferment concentration.
web.lemoyne.edu /~giunta/menten.html   (774 words)

  
 Two Centuries of Catalysis
Although enzymology existed a little earlier, its development was greatly stimulated by Buchner’s discovery, and the first decades of the 20th Century saw the groundwork laid for the study of the kinetics and mechanisms of enzyme action, most notably by Leonor Michaelis and his collaborators.
Nor was Michaelis alone in his high publication rate: Victor Henri, who anticipated him in some respects in our understanding of enzyme action (Henri, 1901), was the author of more than 500 papers, and according to Boyde (1980) his other contributions were always in the first rank.
Before leaving Michaelis it is perhaps appropriate to mention some of his collaborators in the early years of the 20th Century.
bip.cnrs-mrs.fr /bip10/jbiosci.htm   (3159 words)

  
 Michaelis - A GUIDE FOR MICHAELIS-MENTEN ENZYME KINETIC MODELS   (Site not responding. Last check: 2007-09-17)
Using this maximum velocity and equation (7), Michaelis developed a set of The Michaelis constant Km is defined as the substrate concentration at 1/2
Leonor Michaelis: German-American biochemist, born January 16, 1875, Berlin; died October 10, 1949.
This was frist realized by L. Michaelis and ML Menten in 1913, when they developed a quantitative The Michaelis-Menten Kinetic Scheme and Equations
www.toplnk.com /tpl/michaelis.htm   (244 words)

  
 The Michaelis-Menten Equation - Q Fever! - MEDICAL HUMOR
Maude Leonor Menten, a 26-year-old Bavarian chemist, was one of the first women on the scene, looking for love and the meaning of life, and their relation to the velocity of chemical reactions.
Assigned to Suite 243C in the research facility at Alhondiga de Granaditas, she arrived promptly at the lab at 7:30 each morning, and left at 4:30 in the afternoon to carouse the local bars and clubs.
Depressed and alone, he scrapped his plans for the engine and started work on the development of a synthetic substance that could be molded into a cup or bowl, with which he hoped to catch some of the saliva that dribbled daily from the grotesquely loosened right side of his lips.
www.qfever.com /issues/20050810/michaelis-menten.html   (572 words)

  
 Henri-Michaelis-Menten equation (www.whonamedit.com)
This equation gives an expression for the rate of an enzyme reaction and became fundamental to the interpretation of how an enzyme reacts on its substrate.
Before the work of Michaelis and Menten, Victor Henri in 1903 found that enzyme reactions were initiated by a bond between the enzyme and the substrate.
From 1910 Michaelis and Menten took this work further, investigating the kinetics of an enzyme, saccharase, that catalyzes the hydrolysis of sucrose into glucose and fructose.
www.whonamedit.com /synd.cfm/3464.html   (168 words)

  
 Michaelis-Menten equation
As the name implies, these terms are constants, so we can actually combine them into one term.
This new constant is termed the Michaelis constant and is written K
Adding more substrate will not increase the rate of the reaction, hence the levelling out observed in the graph.
www.le.ac.uk /by/teach/biochemweb/tutorials/michment1.html   (1291 words)

  
 Chapter 8 : Enzymes
The kinetic pattern in Figure 8-11 led Victor Henri to propose in 1903 that an enzyme combines with its substrate molecule to form the ES complex as a necessary step in enzyme catalysis.
This idea was expanded into a general theory of enzyme action, particularly by Leonor Michaelis and Maud Menten in 1913.
Michaelis and Menten concerned themselves with the steady-state rate, and this type of analysis is referred to as steady-state kinetics.
www.bioinfo.org.cn /book/biochemistry/chapt08/bio2.htm   (4787 words)

  
 Kinetics of Enzymatic Reactions: The Michaelis-Menten Equation   (Site not responding. Last check: 2007-09-17)
Since the ES concentration is not easily measured experimentally, Leonor Michaelis and Maud Menten have given an alternative expression for the determination of the rate of such enzymatic reactions:
Several algebraic transformations to a linear form have been proposed for this equation which are more useful in the analysis of the experimental data: Lineweaver-Burk, Eadie and Dixon.
The maximum turnover number is the reciprocal of the slope, and the Michaelis constant is the product of the intercept with the maximum turnover number.
www.pmf.ukim.edu.mk /PMF/Chemistry/wmc-rmm1.html   (195 words)

  
 Michaelis-Menten kinetics - Wikpedia   (Site not responding. Last check: 2007-09-17)
Michaelis-Menten kinetics describe the rate of enzyme mediated reactions for many enzymes.
It is named for Leonor Michaelis and Maud Menten.
The relationship between substrate concentration and enzyme concentration was proposed in 1913 by Leonor Michaelis and Maud Menten, following earlier work by Archibald Vivian Hill.
www.bostoncoop.net /~tpryor/wiki/index.php?title=Michaelis-Menten_kinetics   (480 words)

  
 Michaelis - Michaelis-Menten constant (www.whonamedit.com)   (Site not responding. Last check: 2007-09-17)
Calculate the Michaelis constant and the maximum turnover number according the other two equations.
Equation (11), the Michaelis-Menten equation, describes the kinetic behavior of an enzyme that acts according to the simple model (1).
Professor Michaelis and his research group have been studying the brain proteins Michaelis, EK.
findoutpages.com /?q=michaelis   (311 words)

  
 Chapter 7 -- Click Back   (Site not responding. Last check: 2007-09-17)
Leonor Michaelis was born in Berlin in 1875 and received his MD in 1896 from the University of Berlin.
Together in 1913 they developed a rate law, called the Michaelis-Menten Equation that gave the dependence of the rate of substrate consumption –r
From 1929 until his retirement in 1940, Michaelis was a member of the Rockefeller Institute for Medical Research in New York.
www.engin.umich.edu /~cre/course/lectures/seven/biomic.htm   (108 words)

  
 Pitt Chronicle: Maud Who?   (Site not responding. Last check: 2007-09-17)
Menten, who eventually became a professor in the University of Pittsburgh School of Medicine and head of pathology at Children’s Hospital of Pittsburgh, worked with Michaelis to demystify enzyme kinetics—the study of rates and mechanisms of enzymatic reactions.
When Michaelis and Menten published their work in 1913, little was known about enzymes, including their basic chemical nature.
The famous paper she wrote with Michaelis, in which they describe their equation for the first time, refers to her only as “Miss Menten,” according to published reports.
www.discover.pitt.edu /media/pcc050321/womenhistory_maud.html   (1194 words)

  
 Enzymes History Summary   (Site not responding. Last check: 2007-09-17)
German chemist Emil Fischer (1852-1919) recognized the importance of substrate shape for binding by enzymes.
German-American biochemist Leonor Michaelis (1875-1949) and Canadian biologist Maud Menten (1879-1960) introduced a mathematical approach for quantifying enzyme-catalyzed reactions.
American chemists James Sumner (1887-1955) and John Northrop (1891-1987) were among the first to produce highly ordered enzyme crystals and firmly establish the proteinaceous nature of these biological catalysts.
www.bookrags.com /history/genetics/enzymes-wog   (861 words)

  
 JCE Online: Biographical Snapshots: Snapshot
Maude Lenora Menten is best known for her work in enzyme kinetics that describes the relationship between substrate and enzyme in biological systems and gave rise to the Michaelis-Menten equation.
Menten spent one year (1912) at the University of Berlin working with Leonor Michaelis, during which time they derived the Michaelis-Menten equation.
She then went to the University of Chicago, where she obtained a Ph.D. in biochemistry in 1916.
jchemed.chem.wisc.edu /JCEWWW/Features/eChemists/Bios/Menten.html   (472 words)

  
 Canadian Medical Hall of Fame: Laureates   (Site not responding. Last check: 2007-09-17)
Graduating from the University of Toronto in 1913, Menten was one of the first Canadian women to receive a medical degree.
That same year, along with Dr. Leonor Michaelis, Menten introduced a concept that forever changed the study of biological reactions and helped to shape the field of biochemistry.
The Michaelis-Menten equation gave scientists a way in which they could mathematically analyze their observations and descriptions of biological reactions.
www.cdnmedhall.org /laureates?laur_id=36   (204 words)

  
 Michaelis-Menten equation
Observations of this type set Leonor Michaelis and Maud Menten thinking about the underlying reasons why a curve should follow this shape and led them to derive an algebraic equation that now bears their names.
There are several modern ways to explain the way in which the Michaelis-Menten equation is derived, and one is spelt out below.
E binds S to form an enzyme-substrate complex (ES).
www.le.ac.uk /by/teach/biochemweb/tutorials/michment2print.html   (1262 words)

  
 CSHL: Symposia on Quantitative Biology
The participation of current or future Nobel laureates has been a feature of the Symposia and, despite disclaimers to the contrary, has been taken as a measure of the importance of the meetings.
The participants in 1933 set a high standard for subsequent Symposia; Herbert Gasser won a Nobel Prize in 1944, and other eminent participants included Kenneth Cole (nerve conduction), Donald Van Slyke (protein chemist) and Leonor Michaelis (Michaelis-Menten equation).
Through the heroic efforts of Harris, the first volume of the dusky red books was published in December, 1933, just five months after the meeting.
library.cshl.edu /symposia/1933   (371 words)

  
 Maude Leonora Menten   (Site not responding. Last check: 2007-09-17)
Maude Menten, one of the first women doctors in Canada and later a pathologist at the University of Chicago, worked with Leonor Michaelis in experimental support for the kinetic model of enzyme kinetics that we know as the Michaelis-Menten equation (1913).
The equation itself was formulated earlier by Victor Henri (1903) based on poorly controlled experiments on the action of invertase.
The discovery of pH (1909) made it possible for Michaelis and Menten to buffer their reactions, carrying them out under more controlled conditions than had been previously done by Henri and others.
bmbiris.bmb.uga.edu /wampler/8010/lectures/enzyme/menten.html   (116 words)

  
 CORRELATION OF OXIDATION AND PHOSPHORYLATION IN HEMOLYZED BLOOD IN PRESENCE OF METHYLENE BLUE AND PYOCYANINE -- ...
CORRELATION OF OXIDATION AND PHOSPHORYLATION IN HEMOLYZED BLOOD IN PRESENCE OF METHYLENE BLUE AND PYOCYANINE -- Runnström and Michaelis 18 (5): 717 -- The Journal of General Physiology
Articles by Runnström, J. Articles by Michaelis, L. Articles citing this Article
Articles by Runnström, J. Articles by Michaelis, L. The Journal of General Physiology, Vol 18, 717-727, Copyright © 1935 by The Rockefeller University Press
www.jgp.org /cgi/content/abstract/18/5/717   (208 words)

  
 Enzyme Mechanisms   (Site not responding. Last check: 2007-09-17)
The equation describing the kinetics of this system can be derived in a variety of ways; we will simply present it, since your text has all the details:
The expression in this form was first derived by Leonor Michaelis and Maud Menten, and therefore is known as the Michaelis-Menten equation.
The rate of reaction measured as described, in the early stages of reaction, is
chemistry.umeche.maine.edu /CHY431/Enzyme1.html   (431 words)

  
 Untitled   (Site not responding. Last check: 2007-09-17)
Seen by Robert Altmann in 1886 who thought that they were intracellular parasites.
Early workers such as Leonor Michaelis studied mitochondria using the vital dye Janus green.
This dye specifically stains mitochondria in the living cell.
geowww.geo.tcu.edu /bio/couch/biology3603/Ch14lect.html   (1156 words)

  
 Maud Menten   (Site not responding. Last check: 2007-09-17)
Maud Menten became one of the first women doctors in Canada in 1911.
Two years later she and Leonor Michaelis published a paper describing the relationship between the rate of an enzyme-catalysed reaction and the concentration of the enzyme's substrate.
Dr. Menten went on in 1944 to publish on what may be the first use of electrophoresis to seperate proteins.
www.zoo.utoronto.ca /dgwynne/plorch/wis/mm-1.html   (130 words)

  
 Hydrogen Ion Concentration: Its Significance in the Biological Sciences and Methods for Its Determinations - Questia ...   (Site not responding. Last check: 2007-09-17)
Book by Leonor Michaelis, William A. Perlzweig; Williams and Wilkins Company, 1926
Contributors: Leonor Michaelis - author, William A. Perlzweig - author.
Choose a subscription plan to save tons of time, stress and hassle, and do better research, faster.
www.questia.com /PM.qst?a=o&d=96995426   (238 words)

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