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- W1993448469 abstract "Material released from rat mast cells by compound 4880 gave parallel responses using ACTH and β-endorphin radioimmunoassays. However, incubation of these labeled compounds under conditions of radioimmunoassay with released material and chromatography on Sephadex G-25 provided evidence that neither ACTH nor β-endorphin were present in the material released from mast cells, but represented an artifact produced by the presence of a protease. Analysis of the released enzyme on Sephadex G-75 under non-dissociative conditions yielded an active enzyme complex with a Mr > 150,000. Under dissociative conditions, the Mr of the enzyme was 25,000. The dissociated enzyme reassociated with purified rat mast cell heparin to form the high molecular weight complex. Further investigation of pH, substrate and inhibitor specificity showed that the peptide degradation is due to a chymotrypsin-like protease, the previously described mast cell chymase, which is active in degrading β-endorphin, ACTH, and ACTH1–24." @default.
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- W1993448469 date "1981-07-01" @default.
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- W1993448469 title "Peptide hormone degradation by a rat mast cell chymase-heparin complex" @default.
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- W1993448469 doi "https://doi.org/10.1016/0024-3205(81)90333-7" @default.
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