Endopeptidase-24.11 purified from pig intestine is differently glycosylated from that in kidney

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Abstract
Endopeptidase-24.11 (EC 3.4.24.11) was purified from pig intestinal microvilli by immunoadsorbent chromatography, using antibodies raised to kidney endopeptidase-24.11. In many respects, the kidney and intestinal enzymes were indistinguishable, but some structural differences were demonstrated. In particular, the detergent form of the intestinal enzyme had an apparent subunit MW of 95,000, which, on treatment with trypsin, fell to a value of 89,000, identical with that of the kidney form. The intestinal enzyme contained 3-4% more carbohydrate and many more fucose residues than that from kidney. Although these results show that post-translational processing was different in the 2 cell types, the possibility that the primary translation products also differed cannot be excluded.

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