By Gerard Marriott (Eds.)
The seriously acclaimed laboratory normal for greater than 40 years, Methods in Enzymology is without doubt one of the so much hugely revered guides within the box of biochemistry. because 1955, each one quantity has been eagerly awaited, often consulted, and praised through researchers and reviewers alike. greater than 285 volumes were released (all of them nonetheless in print) and masses of the fabric is proper even today--truly a vital book for researchers in all fields of existence sciences
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Reid, J. A. McCray, and D. R. Trentham, Methods in Enzymol. 172, 288-301 (1989). 13 E. Niggli and W. J. Lederer, Biophys. J. 59, 1123-1135 (1991). 4 CAGEDCOMPOUNDS [ 1] that ADP formation by enzyme-induced hydrolysis of ATP was more rapid than the rate of ATP release by photolysis of the caged nucleotide. The presence of ADP, both from enzymatic formation and as an impurity in the caged ATP sample, severely compromised the study. To date, however, the many advantageous properties of 2-nitrobenzyl cages have far outweighed the disadvantages, resulting in a plethora of major applications of 2NB/2NPE chemistry to the study of biochemical mechanisms.
D. Thomas, Biochemistry 30, 8331-8339 (1991). 12 (a) J. W. Walker, G. P. Reid, J. A. McCray, and D. R. Trentham, J. Am. Chem. Soc. 110, 7170-7177 (1988); and (b) J. W. Walker, G. P. Reid, J. A. McCray, and D. R. Trentham, Methods in Enzymol. 172, 288-301 (1989). 13 E. Niggli and W. J. Lederer, Biophys. J. 59, 1123-1135 (1991). 4 CAGEDCOMPOUNDS [ 1] that ADP formation by enzyme-induced hydrolysis of ATP was more rapid than the rate of ATP release by photolysis of the caged nucleotide. The presence of ADP, both from enzymatic formation and as an impurity in the caged ATP sample, severely compromised the study.
Trentham, M. A. Mazid, and M. B. Hursthouse, J. Chem. Soc. Perkin Trans. I, 1015-1019 (1992). 20 j. E. T. Corrie and D. R. Trentham, J. Chem. Soc. Perkin Trans. I, 2409-2417 (1992). 21 M. C. PilTung and S. W. Shuey, J. Org. Chem. 59, 3890-3897 (1994). 22 (a) J. C. Sheehan, R. M. Wilson, and A. W. Oxford, J. Am. Chem. Soc. 93, 7222-7228 (1971); and (b) J. C. Sheehan and J. Umezawa, J. Org. Chem. 38, 3771-3774 (1973). , 10a or 10d) promotes a new, competing photorearrangement process yielding a substituted phenylacetate 11 in addition to the normally encountered acetophenone reduction product 12 [Eq.
Caged Compounds by Gerard Marriott (Eds.)