Read e-book online A guide to protein isolation PDF

By C. Dennison

ISBN-10: 0306468689

ISBN-13: 9780306468681

It's a truism of technology that the extra primary the topic, the extra universally appropriate it really is. however, you will need to strike a degree of “fundamentalness” acceptable to the duty in hand. For -depth examine of the mechanics of motor automobiles might inform one instance, an in not anything in regards to the dynamics of site visitors. site visitors exists on a distinct “level” - it's based upon the lifestyles of motorized vehicles however the physics and arithmetic of site visitors might be competently addressed by means of contemplating motorcars as cellular “blobs”,with no attention of ways they develop into cellular. to begin a discourse on site visitors with a attention of the mechanics of motorized vehicles could hence be inappropropriate. In penning this quantity, i've got wrestled with the query of the right point at which to handle the physics underlying a few of the options utilized in protein isolation. i've got attempted to strike a degree as will be utilized by a mechanic (with probably a mild leaning in the direction of an engineer) - i.e. a pragmatic point, providing applicable perception yet with minimum arithmetic. a few humans occupied with biochemical examine have a minimum grounding in chemistry and physics and so i've got attempted to maintain it so simple as attainable.

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Fugimoto, E. , Goeke, N. , Olsen, B. J. and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85. 14. Wiechelman, K. , Braun, R. D. and Fitzpatrick, J. D. (1988) Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal. Biochem. 175, 231-237. 1 5. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding.

4 A plot of Vo versus [S] yields a so-called substrate dilution curve, such as shown in Fig. 10, which was calculated from the Michaelis-Menten equation, using values of Vmax = 1000 and Km = 90. Figure 10. A substrate dilution curve. Note: The substrate dilution curve must not be confused with the similarly-shaped progress curve. e. that substrate concentration which gives one half of the maximal velocity possible (at that enzyme concentration) is a constant. characteristic for a particular enzyme acting on a particular substrate.

Arch. Biochem. Biophys. 324, 93-98. 5. Perrin, D. D. and Dempsey, B. (1974) Buffers for pH and metal ion control. Chapman and Hall, London. 6. Eisenthal, R. and Cornish-Bowden, A. (1974) The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem. J. 139, 715-720. 7. Segel, I. H. (1976) in Biochemical Calculations, 2nd Ed, John Wiley and Sons, London, pp225-229. 8. Groves, W. , Davis, F. C. and Sells, B. H. (1968) Spectrophotometric determination of microgram quantities of protein without nucleic acid interference.

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