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To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1559-1816.2009.00563.x Byline: Michael P. Leiter (1), Santiago Gascon ([dagger]), Begona Martinez-Jarreta ([dagger]) Abstract: Hospital-based nurses (N = 832) and doctors (N = 603) in northern and eastern Spain completed a survey of job burnout, areas of work life, and management issues. Analysis of the results provides support for a mediation model of burnout that depicts employees' energy, involvement, and efficacy as intermediary experiences between their experiences of work life and their evaluations of organizational change. The key element of this model is its focus on employees' capacity to influence their work environments toward greater conformity with their core values. The model considers 3 aspects of that capacity: decision-making participation, organizational justice, and supervisory relationships. The analysis supports this model and emphasizes a central role for first-line supervisors in employees' experiences of work life. Author Affiliation: (*)Centre for Organizational Research and DevelopmentAcadia UniversityWolfville, Canada ([dagger])School of Occupational MedicineUniversity of ZaragozaZaragoza, Spain Article note: (1) Michael P. Leiter, Centre for Organizational Research and Development, Acadia University, Wolfville, NS, Canada B4P 2J2. E-mail: michael.leiter@acadiau.ca

1. The α-galactosidase of Saccharomyces carlsbergensis is an inducible enzyme which is localized mainly outside the cell membrane and which is secreted into the culture medium in increasing amounts during the growth cycle. 2. The soluble form of α-galactosidase localized inside the cell appears to have the same characteristics as the external one, contrasting with the different forms found in the case of invertase. Although some activity is membrane-bound, this activity, when solubilized with detergent, has the same characteristics as the external form of the enzyme. 3. A procedure has been developed by which the enzyme has been purified using batch adsorption with DEAE-Sephadex and column chromatography in DEAE-Sephadex, DEAE-cellulose and Sephadex G-200, using the supernatant of a culture of Saccharomyces carlsbergensis grown in yeast/ nitrogen base complemented with galactose. 4. The purified enzyme, which is homogeneous by chromatographic criteria and polyacrylamide gel electrophoresis, appears to be glycoprotein. 5. lnvertase copurifies with the α-galactosidase but because of its lower stability, together with the fact that the synthesis of both enzymes can be controlled separately, it was possible to obtain preparations in which the contaminant activity was approximately 1 %. [ABSTRACT FROM AUTHOR]