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• W2083048761 abstract "Abstract 1. 1. Rhynchosciara americana midgut amylase binds chloride ( K d = 1.6 mM at 37°C ) resulting in a 34-fold increase in the Kcat without affecting the Km, but causing a shift in the optimum pH of the enzyme from 6.8 to 8.0. 2. 2. The ions Br−, NO3− and I− also activate the amylase but with a decreasing efficiency. 3. 3. An Arrhenius plot of activity versus temperature show that the amylase display only one slope with a corresponding apparent energy of activation of 4.8 Kcal/mole. 4. 4.|The amylase is a calcium-dependent metalloenzyme which shows a pure competitive inhibition by Hg2+ and a pure non-competitive inhibition by Cu2+ with Ki respectively of 0.21 mM and 0.23 mM. 5. 5.|The resistance to the sulfhydryl reagents p-mercuribenzoate and iodoacetate together with the high Hg2+Ki suggest that sulfhydryl groups are not essential for the midgut amylase activity. 6. 6. Curves of blue-reducing values showed the midgut amylase is an α-amylase with a multiple attack degree between 1.7 and 6. 7. 7. Polyacrylamide gel electrophoresis of midgut homogenates shows the existence of two major isoamylases one of which is largely predominant. 8. 8. The results are compared with α-amylases from several sources." @default.
• W2083048761 created "2016-06-24" @default.
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• W2083048761 date "1977-01-01" @default.
• W2083048761 modified "2023-09-23" @default.
• W2083048761 title "Action pattern, kinetical properties and electrophoretical studies of an alpha-amylase present in midgut homogenates from rhynchosciara americana (diptera) larvae" @default.
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• W2083048761 doi "https://doi.org/10.1016/0305-0491(77)90049-9" @default.
• W2083048761 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11945" @default.
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