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• W1482296368 abstract "Pepsinogen granules were isolated from rabbit stomachs by a combination of differential and isopycnic gradient centrifugation. The isolation procedure utilized 1 M sucrose and alkaline pH to stabilize the granules. The isolated granules were shown to be 8.4-fold enriched in pepsinogen and free of mitochondria and microsome enzyme markers. In addition to pepsinogen, a cation-insensitive but anion-sensitive Mg2+-ATPase co-purified with the zymogen. The enzyme was unaffected by aurovertin, oligomycin, and ouabain, but inhibited by high concentrations of vanadate, N,N'-dicyclohexylcarbodiimide, and azide. The enzyme activity was stimulated by tetrachlorosalicylanilide and the combination of valinomycin and nigericin in K+-containing media. The similarities between this enzyme and other secretory granule ATPases are discussed." @default.
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• W1482296368 date "1984-07-01" @default.
• W1482296368 modified "2023-10-18" @default.
• W1482296368 title "Isolation of pepsinogen granules from rabbit gastric mucosa." @default.
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• W1482296368 doi "https://doi.org/10.1016/s0021-9258(17)47293-0" @default.
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