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Isolation of Amylopectin Granules and Identification of Amylopectin Phosphorylase in the Oocysts of Eimeria tenella
Author(s) -
WANG C. C.,
WEPPELMAN R. M.,
LOPEZRAMOS B.
Publication year - 1975
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1975.tb05233.x
Subject(s) - amylopectin , maltose , biology , biochemistry , glycogen phosphorylase , eimeria , enzyme , microbiology and biotechnology , amylose , starch
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 10 6 unsporulated oocysts and 93 nmoles maltose from those from 10 6 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 K m 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.