. Biophysical science. Biophysics. Figure I. The concentration of the substrate S of a hydrolytic reaction as a function of time. This is actually Figure 2. The rate of disappear- ance of S as computed from the curve at left. However, a graph of the rate of the enzyme catalyzed reaction plotted against [S] shows that at higher concentrations the term k in Equation 1 is not constant. Similar studies show that this k is propor- tional to the enzyme concentration at low concentrations but not at high enzyme concentrations. This situation is illustrated in Figures 1, 2, 3, and 4. Michae
. Biophysical science. Biophysics. Figure I. The concentration of the substrate S of a hydrolytic reaction as a function of time. This is actually Figure 2. The rate of disappear- ance of S as computed from the curve at left. However, a graph of the rate of the enzyme catalyzed reaction plotted against [S] shows that at higher concentrations the term k in Equation 1 is not constant. Similar studies show that this k is propor- tional to the enzyme concentration at low concentrations but not at high enzyme concentrations. This situation is illustrated in Figures 1, 2, 3, and 4. Michaelis and Menten pointed out that this failure to obey the prediction of Equation 1 could easily be explained if the reaction mechanism were oversimplified. A simple scheme which they proposed is to assume that the enzyme and substrate formed an intermediate. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Ackerman, Eugene, 1920-. Englewood Cliffs, N. J. , Prentice-Hall
Size: 1576px × 1585px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookcentury1900, bookcollectionbiodiversi, booksubjectbiophysics
