Abstract
THE heritable connective tissue disease in cattle called dermatosparaxis is characterized by extreme fragility of the skin1,2. This anomaly is presumably due to abnormal collagen fibres which, on analysis, are found to contain a substantial amount of procollagen3. The mutation has been attributed to the absence of an enzyme, procollagen peptidase, which removes a non-collagenous amino terminal peptide from the procollagen molecule, yielding “finished” collagen molecules4. Some normal collagen is present in the mutant tissues, indicating either that the mutation is incomplete, or that proteases, from other cells, may participate in procollagen processing.
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