Methods in Enzymology Vol.45 Proteolytic Enzymes, Part B

Discussion in 'Methods in Enzymology Book Series' started by admin, Jul 18, 2016.

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    admin Thư Viện Sách Việt Staff Member Quản Trị Viên

    This chapter discusses the complications related to immobilize enzymes while determining of the kinetic constants. The measurement of the kinetic constants of immobilized enzymes may not yield true values equivalent to those obtained in homogeneous reactions, because of the influence of physical factors, such as diffusion. Hence, rate and binding constants should be referred to as apparent Vmax and apparent Km and written as Vmax (app) and Km (app). An operational definition of Km (app) would be that substrate concentration which gives a reaction velocity corresponding to half the Vmax (app). It is suggested that immobilized enzymes generally show less specific activity than the native enzyme. Losses in activity are minimized because more sophisticated procedures have being developed. In characterizing immobilized enzymes, the activity should ideally be expressed as the initial reaction rate in terms of for instances microkatals per milligram of dry immobilized enzyme preparation or any multiple thereof.
    • Hardcover: 939 pages
    • Publisher: Academic Press; 1 edition (January 11, 1977)
    • Language: English
    • ISBN-10: 0121819450
    • ISBN-13: 978-0121819453
    • Product Dimensions: 6 x 2 x 9 inches
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    Last edited: Jul 2, 2022

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