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Just Published! Industry's Future: Changing Patterns of Industrial Research This fascinating volume -AMMgMg. ,. : provides the readers with Changing Patterns of Industrial Research an under­ standing of the dynamic processes that make industrial research a Herbert I. Fusfeld principal driving force in creating technical change, producing economic growth, and strengthening the technical institu­ tions in society. It describes and analyzes the major factors that shape the conduct and organization of industrial research, including the internationalization of R&D, restructuring of industry, declining defense expenditures and the pressure to develop access to sources of technical change outside the corporation. The volume presents approaches for improved industry relations with government and academia, discusses complex conditions for conducting industrial research effectively and analyzes potential new conditions that can shape future industrial research. The experiences of specific corporations with modern manage­ ment of technology are also de­ scribed. Herbert I. Fusfeld

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384 pages (1994) Clothbound: ISBN 0-841 2-2983-X $39.95 Paperbound: ISBN 0-8412-2984-8 $24.95

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Report^ power and wavelength, matrix, and rf voltage on the ring electrode. We found this to be the case for the peptide angiotensin III. The spectrum was obtained following MALDI activation at 355 nm and a trap storage time of 50 ms so that decay was complete. The laser power, trapping, and ejection conditions were optimized for ion fragmentation at the ex­ pense of resolution. The ion decay pro­ vides a nearly complete set of b and b 1 7 peaks for sequencing under these condi­ tions. Similar results have been obtained for a number of peptides including substance P, neurotensin, angiotensin I, bradykinin, and melittin. In most cases a rela­ tively complete set of b or y fragments is observed. However, it is significant that the decay is completed within the trap so that the long-lived decay is observed as stable peaks in one complete spectrum from the reTOF spectrometer. In postsource decay reTOF experiments the de­ cay is detected as metastable ions and the reflectron energy analyzer must be scanned over an extended period to obtain a complete spectrum. Outlook There are currently 15-20 IT/reTOF spectrometers of varying designs in labo­ ratories around the world. Although the published literature still remains sparse on this relatively new mass spectrometric instrument, we expect that the need for fast response, high sensitivity, and struc­ tural analysis in chromatographic detec­ tion will make the IT/reTOF spectrome­ ter the analyst's instrument of choice in such applications. We thank Michael Lang and Robert Stetler (for the loan of software and other equipment) and S. E. Buttrill, Jr. (for a critical reading of the manuscript) of Varian. We gratefully acknowl­ edge the National Science Foundation, the Na­ tional Center for Human Genome Research, and Varian Associates, Inc., Ginzton Research Center.

Kaiser, R E., Jr.; Schwartz, J. C. Rapid Comm. Mass Spectrom. 1991,5,327-29. (5) Michael, S. M.; Chien, B. M.; Lubman, D. M. Anal. Chem. 1993, 65, 2614-20. (6) Boesl, U.; Neusser, H. J.; Weinkauf, R; Schlag, E. W./. Phys. Chem. 1982,86, 4857-63. (7) Lubman, D. M.; Jordan, R. M. Rev. Set. Instrum. 1985,56,373-76. (8) Opsal, R. B.; Owens, K. G.; Reilly, J. P. Anal. Chem. 1985,57,1884-89. (9) Kinsel, G. R; Grundwuermer, J. M.; Grotemeyer, ].]. Am. Soc. Mass Spectrom. 1993,4,2-10. (10) Colby, S. M.; King, T. B.; Reilly, J. P. Rapid Comm. Mass Spectrom. 1994,8,865-68. (11) Cooks, R. G.; Kaiser, R. E., Jr. Ace. Chem. Res. 1990,23,213-19. (12) Nourse, B. D.; Cooks, R. G. Anal. Chem. Acta 1990,228,1-21. (13) Cornish, T. J.; Cotter, R J. Rapid Comm. Mass Spectrom. 1993, 7,1037-40. (14) Cooks, R J.; Glish, G. L.; McLuckey, S. A; Kaiser, R E., Jr. Chem. Eng. News, March 25,1991, pp. 26-41. (15) Mosburg, E. R.; Vedel, M.; Zeraga, Y.; Vedel, F.; Andre, J. Int. J. Mass Spectrom. Ion Proc. 1987, 77,1-12. (16) Lifshitz, C; Nadav, E.; Peres, M.; Peres, T.; Laskin, J.; Karsenty, B.; Shaked, M. Int. J. Mass Spectrom. Ion Proc. 1994,133, L11-L14. (17) Suter, M.J.F.; Gfeller, H.; Schlunegger, U. P. Rapid Comm. Mass Spectrom. 1989, 3,62-66. (18) Fenn, J. B.; Mann, M.; Meng, C. K; Wong, S. F.; Whitehouse, C. M. Science 1989, 246, 64-71. (19) Chien, B. M.; Lubman, D. M. Anal. Chem. 1994,66,1630-36. (20) Boyle, J. G.; Whitehouse, C. M. Anal. Chem. 1992, 64, 2084-89. (21) Mirgorodskaya, O. A; Shevchenko, A A; Chernushevich, I. V.; Dodonov, A. F.; Miroshnikov, A I. Anal. Chem. 1994, 66, 99-107. (22) Verentchikov, A N.; Ens, W.; Standing, K. G. Anal. Chem. 1994, 66,126-33. (23) Smith, R. D.; Loo, J. A; Barinaga, C. J.; Ed­ monds, C. G.; Udseth, H. R/. Am. Soc. Mass Spectrom. 1990,1,54-65. (24) Chien, B. M.; Michael, S. M.; Lubman, D. M. Rapid Comm. Mass Spectrom. 1993, 7, 837-43. (25) Fountain, S. T.; Lee, H.; Lubman, D. M. Rapid Commun. Mass Spectrom. 1994,8, 407-16. (26) Spengler, B.; Kirsch, D.; Kaufmann, R. /. Phys. Chem. 1992, 96, 9678-84.

David Lubman's research interests include protein and DNA sequencing, instrument design, and bacterial screening. Mark Qian's research interests focus on LC/MS References instrumentation, high-resolution electro­ (1) Cotter, R J. Anal. Chem. 1992, 64,1027 phoresis, and separation and characteriza­ A-1039A. tion of proteins and low molecular weight (2) Chambers, D. M.; Goeringer, D. E.; McLuckey, S. A; Glish, G. L. Anal. Chem. compounds of biomedical interest. Address 1993, 65,14-20. correspondence about this article to Lub­ (3) McLuckey, S. A; Van Berkel, G. J.; Go­ man at the Department of Chemistry, The eringer, D. E.; Glish, G. L. Anal. Chem. University of Michigan, Ann Arbor, MI 1994, 66,689 A-696 A 48109. (4) Cooks, R G.; Williams, J. D.; Cox, Κ A;

Analytical Chemistry, Vol. 67, No. 7, April 1, 1995