Intracellular Distribution of Proteolytic Enzymes in Rat Liver Tissue.

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Abstract
Rat liver tissue was homogenized in sucrose solutions and separated into various particulates by differential centrifugation. By using benzoyl-L-argininamide and glycyl-L-tyrosinamide as substrates it was demonstrated that the activity of cathepsins B and C is localized in the mito-chondrial fraction of these same homogenates. This phenomenon may be the consequence of the removal of an inhibitor or inhibitors present in the supernatant fluid of the homogenates. Certain characteristics of the inhibiting substance are given.

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