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- W2005017809 abstract "Analytical expressions describing steady-state kinetics are given for systems with enzymes enclosed or covalently bound in spherical gel particles. In experiments using immobilized CT∗ the rate of product formation was found to be proportional to the square root of the enzyme content at low substrate concentration, and proportional to the enzyme content at high substrate content. These findings are in agreement with the results predicted from the theoretical model. The determination of the turnover number and Michaelis-Menten constant for immobilized enzymes is outlined. Some possible consequences for the description of enzyme kinetics in vivo are discussed." @default.
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- W2005017809 date "1971-11-01" @default.
- W2005017809 modified "2023-10-18" @default.
- W2005017809 title "A theoretical model describing steady-state catalysis by enzymes immobilized in spherical gel particles. Experimental study of α-chymotrypsin-sepharose" @default.
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- W2005017809 doi "https://doi.org/10.1016/0006-291x(71)90461-x" @default.
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