Direct observation of binding between biotinylated okadaic acids and protein phosphatase 2A monitored by surface plasmon resonance

Tetrahedron Letters

Volumn 40, Issue 5, 1999, Pages 887-890

  Konoki, Keiichi ^a   Sugiyama, Naoyuki ^a   Murata, Michio ^a   Tachibana, Kazuo ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Okadaic acid; Protein phosphatases; Surface plasmon resonance

Indexed keywords

OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A;

ARTICLE; BINDING AFFINITY; CATALYSIS; DRUG RECEPTOR BINDING; DRUG SYNTHESIS; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIGAND BINDING; PROTEIN DNA BINDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SURFACE PLASMON RESONANCE;

EID: 0033613772     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(98)02474-5     Document Type: Article

References (27)

1. K. Tachibana, P. J. Scheuer, Y. Tsukitani, H. Kikuchi, D. V. Engen, J. Clardy, Y. Gopichand, and F. J. Shumitz, J. Am. Chem. Soc. 1981, 103, 2469-2470.
2. (a) M. Suganuma, H. Fujiki, S. Okabe, S. Nishiwaki, D. Brautigan, T. S. Ingebritsen, and M. R. Rosner, Toxicon 1992, 30, 873-878.
3. (b) H. Fujiki and M. Suganuma, Adv. Cancer Res. 1993, 61, 143-194.
4. (a) M. Suganuma, M. Suttajit, H. Suguri, M. Ojika, K. Yamada, and H. Fujiki, FEBS Lett. 1989, 250, 615-618.
5. (b) S. Nishiwaki H. Fujiki, M. Suganuma, M. Ojika, K. Yamada, and T. Yasumoto, Biochem. Biophys. Res. Commun. 1990, 170, 1359-1364.
6. (a) C. Bialojan and A. Takai, Biophys. J. 1988, 256, 283-290.
7. (b) A. Takai and G. Mieskes, Biochem. J. 1991, 275, 233-239.
8. (a) S. Löyfås and B. Johnsson, J. Chem. Soc., Chem. Commun. 1990, 21, 1526-1528.
9. (b) R. Karlsson, A. Michaelsson, and L. Mattson, J. Immunol. Methods 1991, 145, 229-240.
10. (c) S. SjölAnder and C. Urbaniczky, Anal. Chem. 1991, 63, 2338-2345.
11. (d) B. Johnsson, S. Löfäs, and G. Lindquist, Anal. Biochem. 1991, 198, 268-277.
12. (e) R. Karlsson, A. Michaelsson, and L. Mattsson, J. Immnol. Methods 1991, 145, 229-240.
13. (f) L. G. Fägerstam, Å. F.-Karlsson, R. Karlsson, B. Persson, and I. Rönnberg, J. Chromatography 1992, 597, 397-410.
14. 5a) to the dextran surface of a sensor chip (CM5), which possesses carboxylic acid groups. However, interactions of these immobilized enzymes with neither 1 nor the biotin conjugates of 1 was detected, probably because of the insignificant changes in SPR due to the much smaller molecular weight of the analyte, compared with the enzymes.
15. Methods in Enzymology, 184, eds. M. Wilchek and E. A. Bayer, Academic Press, Sandiego, 5-13 (1990).
16. 3N, and removing the tert-butyloxy carbonyl group with trifluoroacetic acid (52% yield in 2 steps).
17. 2-).
18. T. Yanagi, M. Murata, K. Torigoe, and T. Yasumoto, Agric. Biol. Chem. 1989, 53, 525-529.
19. J. Inanaga, K. Hirata, H. Saeki, T. Katsuki, and M. Yamaguchi, Bull. Chem. Soc. Jpn. 1979, 52, 1989-1993.
20. S. Neelakuntan, R. Padmasani, and T. R. Seshadri, Tetrahedron 1965, 21, 3531-3536.
21. A. K. Ghosh, T. T. Duong, S. P. McKee, and W. J. Thompson, Tetrahedron Lett. 1992, 33, 2781-2784.
22. 18) From the close spectral resemblance between 1 and 5, the signals at δ 4.24 and δ 4.13 were assignable to H-24 and H-27, respectively, and these virtually unchanged chemical shifts between 1 and 5 ruled out their acyl substitutions.
23. 3 at a flow rate of 5 μL/min for 180 sec. The running buffer consisted of 150 mM NaCl, 3.4 mM EDTA, 0.01% Tween® 20, 0.02% (w/v) BSA and 10 mM Hepes/NaOH (pH 7.4). All experiments were carried out at 25 °C.
24. (a) S. Nishiwaki, H. Fujiki, M. Suganuma, H. Furuya-Suguri, R. Matsushima, Y. Iida, M. Ojika, K. Yamada, D. Uemura, T. Yasumoto, F. J. Schmitz, andT. Sugimura, Carcinogenesis 1990, 11, 1837-1841.
25. (b) A. Takai, M. Murata, K. Torigoe, M. Isobe, G. Mieskes, and T. Yasumoto, Biochem. J. 1992, 284, 539-544.
26. 16)
27. T. Yasumoto, M. Murata, Y. Oshima, M. Sano, G. K. Matsumoto, J. Clardy, Tetrahedron 1985, 41, 1019-1025.