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. 1987 Dec 1;248(2):345–350. doi: 10.1042/bj2480345

Neutral endopeptidase-24.11 (enkephalinase). Biosynthesis and localization in human fibroblasts.

G Lorkowski 1, J E Zijderhand-Bleekemolen 1, E G Erdös 1, K von Figura 1, A Hasilik 1
PMCID: PMC1148547  PMID: 3481263

Abstract

The biosynthesis, glycosylation and subcellular localization of the neutral endopeptidase-24.11 were studied in cultured human fibroblasts. The enzyme was synthesized as a precursor (Mr 88,000) containing four or five N-linked oligosaccharides. Within 1 h the synthesis-mature (Mr 94,000) endopeptidase-24.11 was formed and contained sialylated oligosaccharides. The half-life of endopeptidase-24.11 was 3.7 days and in the presence of 10 mM-NH4Cl it increased to 6 days. Mature endopeptidase-24.11 was solubilized with 0.2% saponin and partitioned into Triton X-114. In intact fibroblasts, endopeptidase-24.11 was accessible to antibodies and to neuraminidase even when the treatment was performed at 4 degrees C. The localization of endopeptidase-24.11 to the plasma membrane in cultured fibroblasts was further demonstrated by immunocytochemistry.

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