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- W2024793513 abstract "SYNOPSIS. Amylopectin granules were purified from Eimeria tenella oocysts following digestion with sodium dodecyl sulfate and pronase. The oval granules had a uniform size of 0.5 × 0.7 μm, and consisted of only glucose polymers. α-Amylase treatment yielded 235 nmoles of maltose from the granules from 106 unsporulated oocysts and 93 nmoles maltose from those from 106 sporulated oocysts. Amylopectin phosphorylase activity was detected in the cytoplasm of unsporulated oocysts of E. tenella. It had a specific activity of 13 U/mg protein in crude extracts, and a pH optimum of 6.0. The Km values determined were 9.1 mM for glucose-1-phosphate and 5.6 mM for glucose end groups in potato amylopectin. Enzyme activity declined at a linear rate during sporulation, sporulated oocysts containing less than 8% of the activity of unsporulated oocysts. No amylase-type activity was found in the parasite." @default.
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- W2024793513 date "1975-11-01" @default.
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- W2024793513 title "Isolation of Amylopectin Granules and Identification of Amylopectin Phosphorylase in the Oocysts of<i>Eimeria tenella</i>" @default.
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- W2024793513 doi "https://doi.org/10.1111/j.1550-7408.1975.tb05233.x" @default.
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