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- W2045502904 abstract "Cathepsin D (EC 3.4.3.23) purified from human putuitary by affinity chromatography on pepstatin-Sepharose cleaved human β-endorphin (LPH 61–91) at the Leu77-Phe78 bond after incubation at pH 3.2 for 1–3. Incubation with smaller lipotropic fragments (enkephalin, α-endorphin, β-endorphin) did not lead to further degradation. Cleavage sites were identified following the separation of danyslated or iodinated peptides on polyamide sheets accompanied by N-group determination, or following slab-gel electrophoresis of the iodinated peptides. Cleavage at the above site was blocked using an analog containing D-Leu77. Breakdown of porcine β-lipotropin (LPH 1–91) was slower and required an 18 h incubation. A product LPH 1–77 was tentatively identified based in part on its mobility on slab gels as compared to β-LPH and β-endophine and by N-group determination of cleavage products." @default.
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- W2045502904 date "1978-11-01" @default.
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- W2045502904 title "Conversion of lipotropic peptides by purified cathepsin D of human pituitary: Release of γ-endorphin by cleavage of the Leu77-PHE78 bond" @default.
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- W2045502904 doi "https://doi.org/10.1016/0304-3940(78)90003-4" @default.
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