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A sample of 199 project management personnel took the Myers-Briggs Type Indicator and the Thomas-Kilmann Conflict Mode instrument. Results supported the earlier research of Thomas and Kilmann (1975) with two extensions. Extraversion in our sample was not associated with cooperation, and it correlated with both the distributive and integrative dimensions of conflict handling.

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23) Katakuse, I.; Nakabushi, H.; Ichihara, T.; Sakurai, T.; Matsuo, T.; Matsuda, H. Int. J . Mass Spectrom. Ion Proc. 1984, 62, 17. (24) Morgan, T. G.; RabrenoviE, M.; Harris, F. M.; Beynon, J. H. Org. Mass (32) Castro, M. E.; Mallis, L. M.; Russell, D H. J Am. Chem. SOC. 1985, 107, 5652. (33) Mallis, L. M.; Russell, D. H., unpublished results. (34) Castro, M. E.; Mallis, L. M.; Russell, D. H., unpublished results. (35) Castro, M. E.; Russell, D. H. Fast atom bombardment mass spectrometry was used to provide quantitative analytical data for the calculation of kinetic parameters for the action of trypsin on several small peptides. The method provides a unique capability in that spectfic molecular species may be followed independently of other components'in the mixture. The analysis takes place within minutes of sampling the reaction and does not require any cleanup or chemical derivatiratlon procedures prior to analysis. The method is illustrated by determining K, and k,, for the hydrolysis of several peptides by trypsin. These results are compared with values for similar peptides that have been reported in the literature.The determination of kinetic constants of enzymes for specific substrates has involved the use of a variety of analytical methods, which usually include spectroscopic and chromatographic techniques as primary quantitative tools. Much of this information has been obtained through the study of substrate analogues and chemically modified natural substrates in order to provide compounds that can be followed in the enzyme reaction with high sensitivity and specificity.Present address: Proctor a n d Gamble Corp., Cincinnati, OH.For example, kinetic constants for trypsin have been determined by using tosylarginine methyl ester and benzoylarginine ethyl ester, as well as various analogues. Although these data serve a valuable role in providing comparative kinetic constants for small substrates and the convenient assay of these enzymes, they do not necessarily represent constants that may be reasonably applied to estimate those for natural substrates.Work done thus far in the determination of K , for trypsin using specific peptide substrates has given values that are much greater than those for many synthetic substrates (1-3). For other enzymes, such data are sparse due to the difficulties encountered with the appropriate analytical methodology.Fast atom bombardment mass spectrometry (FABMS) is emerging as a powerful analytical tool for biomolecular analysis in studies involving the determination of ionic constituents in aqueous solutions (4). For enzyme kinetic studies, FABMS provides several basic capabilities. First, it has a very high degree of molecular specificity in that the mass spectrum can identify individual molecular species in mixtures, including specific charged forms of a given compound. Second, it can analyze most compounds directly in reaction mixtures without chemical derivatization and separation steps. Third, it is a very sensitive technique, which most often requires only a few nanomo...