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  • Title: A neutral proteinase from human gingival fibroblasts active against the c-terminal cross-linking region of type I collagen.
    Author: Scott PG, Goldberg HA, Dodd CM.
    Journal: Biochem Biophys Res Commun; 1983 Aug 12; 114(3):1064-70. PubMed ID: 6311193.
    Abstract:
    An enzyme that was capable of releasing small fragments containing hydroxynorleucine from the c-terminal extra-helical region of the alpha 1 chain of reduced (tritiated) soluble type I collagen was found, along with collagenase, in medium that had been conditioned by the culture of human gingival fibroblasts (Gin-1). The enzyme was present in a latent form or forms and could be activated by treatment with either trypsin or p-hydroxymercuribenzoate. It was maximally active at neutral pH and inhibited by EDTA. It is suggested that this enzyme, acting within a region of the molecule which is of major importance in stabilizing fibrillar collagen through intermolecular cross-linking, could potentially play an important role in collagen turnover in vivo.
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