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- W2045595005 abstract "Proteolytic activity was detected in crude extracts of female reproductive accessory glands and the following characteristics of the principal aminopeptidase activities were determined: substrate specificity, pH optima, molecular weights, and effects of inorganic salts. The greatest aminopeptidase activities were found with the β-naphthylamides of: alanine at pH 7.5 and 9.5, leucine at pH 8.0, and methionine at pH 6.5. The methionine-specific activity in the crude extract was stimulated 3 times by 100 mM MgCl2, CaCl2, NaCl, or KCl. Inhibition was noted, and ID50 was determined for each of the other principal substrates with the following salts: CdCl2, CaCl2, ZnCl2, HgCl2, MgCl2, and MnCl2. Molecular weights, estimated on Sephadex G-200 and on Sepharose-6B, were found to be around 210 000 for each of these principal aminopeptidase activities in the crude extract." @default.
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- W2045595005 date "1983-08-01" @default.
- W2045595005 modified "2023-09-27" @default.
- W2045595005 title "Characteristics of aminopeptidase activity of female housefly reproductive accessory glands" @default.
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- W2045595005 doi "https://doi.org/10.1080/01651269.1983.10510028" @default.
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