Download e-book for kindle: Affinity labeling by Nathan P. Kaplan, Nathan P. Colowick, William B. Jakoby,

By Nathan P. Kaplan, Nathan P. Colowick, William B. Jakoby, Meir Wilchek

ISBN-10: 0121819469

ISBN-13: 9780121819460

The significantly acclaimed laboratory regular, Methods in Enzymology, is likely one of the such a lot hugely revered courses within the box of biochemistry. for the reason that 1955, every one quantity has been eagerly awaited, often consulted, and praised by way of researchers and reviewers alike. The sequence includes a lot fabric nonetheless correct at the present time - really a necessary ebook for researchers in all fields of existence sciences

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Biochem. , in press. ~sK. D. Collins, J. Biol. Chem. 49, 136 (1974). ~"G. E. Lienhard and I. I. Secemski, J. Biol. Chem. 248, 1121 (1973). 28 Although binding ratios as large as 105-106 are found in some cases, it should be emphasized that true Ks values are not often known for productive ES complexes, and may be higher or lower than the observed K~ values on which the apparent binding ratios are based. In addition, it seems probable that calculations according to expressions such as Scheme 2 provide only an upper limiting value for KTx, in the likely event that the enzymic and nonenzymic reactions differ in the detailed structure of the altered substrate in the transition state2 Affinity Labeling with Transition State Analogs The possibility of combining the features of a transition state analog with those of an affinity labeling agent remains to be explored in detail, but it appears to have been realized unexpectedly in two cases.

122, 727 (1971). k D. H. Buttlaire and M. Cohn, J. Biol. Chem. 249, 5733 (1974). K. A. Koetfler and G. P. Hess, Biochemistry 18, 5345 (1974). K. A. Koehler and G. E. Lienhard, Biochemistry 10, 2477 (1971). R. N. Lindquist and C. Terry, Arch. Biochem. Biophys. 160, 135 (1974). ° J. O. Westerik and R. Wolfenden, J. Biol. Chem. 247, 8195 (1971). P R. C. Thompson, Biochemistry 12, 47 (1973). J. O. Westerik a n d R . Wolfenden, J. Biol. Chem. 249, 6351 (1974). r j. D. Findlater and B. A. Orsi, FEBS Left.

Wolfenden, unpublished results. 1, R. C. Thompson, Biochemistry 13, 5495 (1974). 1, W. B. Novoa, A. D. Winer, A. J. Glaid, and G. W. Schwert, d. Biol. Chem. ~ 4 , 1143 (1959). 18E. Racker, V. Klybas, and M. Schramm, d. Biol. Chem. 234, 2510 (1958). ~A. L. Fluharty and C. E. Ballou, J. Biol. Chem. 234, 2517 (1958). ~R dehydrogenase ] H~,.. e. o. o- -ope| hh (CH2)2 NH~--C--COOH H a j. Everse, E. C. Zoll, L. Kahan, and N. O. Kaplan, Bioorg. Chem. 1, 207 (1971). b W. B. Noroa, A. D. Winer, A. J. Glaid, and G.

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Affinity labeling by Nathan P. Kaplan, Nathan P. Colowick, William B. Jakoby, Meir Wilchek


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