Modified properties of hexokinase from heart mitochondria prepared using proteolytic enzyme |
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Authors: | E Aubert-Foucher B Font D C Gautheron |
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Institution: | (1) Laboratoire de Biologie et Technologie des Membranes du CNRS, Universite Claude Bernard, 69622 Villeurbanne Cedex, France;(2) Laboratoire de Biologic et de Technologie des Membranes du CNRS, Université Claude Bernard, 69622 Villeurbanne Cedex, France |
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Abstract: | Summary Isolation of muscle mitochondria is made easier by using proteolytic treatment of the tissue before homogenization. Normally,
the proteolytic enzyme is discarded with the supernatant of the first centrifugation. However, our results show that a fraction
of enzyme activity remains associated with mitochondria. As shown in experiments described in this paper, mitochondrial hexokinase
from tissue treated or not with the proteolytic enzyme exhibits similar properties except that the solubilized enzyme from
protease treated tissue is no longer able to rebind to mitochondrial membrane. This modification of the binding ability of
the enzyme results from a partial hydrolysis of hexokinase during solubilization experiments by the proteolytic enzyme.
Since, as pointed out here, proteolytic enzyme can remain associated with mitochondria, either adsorbed on mitochondrial
membrane or included in the mitochondrial pellet] its use for the isolation of muscle mitochondria should be avoided. |
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Keywords: | Proteolytic enzyme enzyme membrane interactions heart mitochondria hexokinase |
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