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  • Termitomyces clypeatus  (1)
  • bilateral relationships  (1)
  • 2010-2014
  • 1995-1999  (2)
  • 1995  (2)
Collection
Publisher
Years
  • 2010-2014
  • 1995-1999  (2)
Year
  • 1995  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Marketing letters 6 (1995), S. 33-44 
    ISSN: 1573-059X
    Keywords: exclusivity ; bilateral relationships ; comarketing alliances ; channels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Economics
    Notes: Abstract In bilateral interorganizational relationships, individual firm's self-interest is subordinate to the larger interest of the collective system. Bilateral governance is facilitated by exclusivity under certain conditions. Exclusive relationships draw partners closer and improve coordination. However, exclusivity leads to a loss of flexibility in dealing with turbulent environments. We test relationships between exclusivity and antecedent variables from transaction-cost analysis, resource-dependence theory, and organization theory. We find that while relationship-specific investment calls for more exclusivity, interdependence and rapid technological change call for less. Further, in the computer and semiconductor industry, exclusivity is negatively related to perceived effectiveness. Hence exclusivity should be used judiciously in the management of bilateral interrorganizational relationships.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 359-360 
    ISSN: 1573-0972
    Keywords: α-L-Arabino furanosidase ; Termitomyces clypeatus ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Termitomyces clypeatus produced xylanase and α-L-arabinofuranosidase simultaneously in various media. The arabinofuranosidase had pH and temperature optima of 5.5 and 50°C, respectively, and was stable at 50°C for 30 min and at pH values from 2 to 5. The partially purified enzyme was distinct from xylanase present in the same medium.
    Type of Medium: Electronic Resource
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