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Enzymes Covalently Bound on Collagen Membranes Immobilization of Blood Clotting Factor XIII

  • Danièle C. Gautheron
  • Bruno G. Blanchy
  • Pierre R. Coulet
Part of the Advances in Experimental Medicine and Biology book series (AEMB)

Abstract

Ever since 1958 I have specialized in the field of mitochondrial research: metabolism, structure of inner mitochondrial membrane, ATP synthase. Therefore one can wonder why I started binding enzymes to collagen membranes and why we specially immobilized Factor XIII in this type of thin membranes, since we had no competence concerning blood clotting in the Laboratory. In fact, in a first approach, with J.H. Julliard, hand-made ultra-thin films of collagen were prepared in the Laboratory and used for the covalent binding of glutamate dehydrogenase by an azide method to make a simple model of interactions of glutamate dehydrogenase with inner mitochondrial membrane1. Glutamate dehydrogenase is an abundant mitochondrial enzyme that strongly interacts specifically with the inner face of the inner mitochondrial membrane, therefore from the matrix side. If the kinetic parameters of the enzyme were somewhat modified, however, the bound glutamate dehydrogenase kept its cooperative properties and regulations by the effectors ADP and GTP. This meant that the bound enzyme had kept its specific oligomeric structure and organization. It was such a success that we decided to develop the system.

Keywords

Glutamate Dehydrogenase Covalent Binding Factor Xiii Adenylate Kinase Collagen Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Danièle C. Gautheron
    • 1
  • Bruno G. Blanchy
    • 1
  • Pierre R. Coulet
    • 1
  1. 1.Laboratoire de Biologie et Technologie des MembranesCNRS — Université Claude Bernard de LyonVilleurbanne CedexFrance

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