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The Three Cortical Membranes of the Gregarines (Parasitic Protozoa). III. Comparative Studies of the Membrane Proteins Among Different Sporozoan Species During Their Vegetative Phase 1
Author(s) -
PHILIPPE M.,
VINCKIER D.,
DUBREMETZ J. F.,
SCHREVEL J.
Publication year - 1982
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.1550-7408.1982.tb05426.x
Subject(s) - biology , glycoconjugate , electrophoresis , polyacrylamide gel electrophoresis , staining , biochemistry , protozoa , gel electrophoresis , ultrastructure , botany , genetics , enzyme
. The cortical membrane proteins of three gregarine and one coccidian species were compared using sodium dodecyl sulfate/polyacrylamide‐gel electrophoresis. About 30 proteins were identified in the ghosts of Gregarina blaberae and G. garnhami and 20 in G. rhyparobiae ghosts and Sarcocystis tenella pellicles. No protein with the electrophoretic mobility of muscular actin was present in the ghosts of the sporozoan species under study. Each species possessed a characteristic electrophoretic pattern; no protein was present simultaneously in the four sporozoan species and only one protein band with a similar electrophoretic mobility was found in the three gregarine species (52 Kd protein). Two G. garnhami subpopulations living in Locusta migratoria and Schistocerca gregaria exhibited the same ghost protein pattern. Thus, large differences were observed between species and not within species, and the protein electrophoretic analysis appears to be a powerful tool for taxonomic investigations in gregarines. Gregarina blaberae and G. garnhami glycoconjugates were compared after periodate/Schiff staining of the polyacrylamide gel slabs. Several glycoconjugates were reported to belong to the cytoplasmic fraction; and, in view of cytochemical and ultrastructural data, a contribution of these glycocomponents to the secretion of a mucus is discussed.