title: [Number, activity and thermostability of the electrophoretic forms of acid phosphatase in Amoeba proteus, cultured at different temperatures].
abstract: In free-living amoebae (Amoeba proteus, strain B), cultured at 10 and 25 degrees C, we compared the number, activity, and thermostability of separate electromorphs of Triton-soluble acid phosphatase (AcP) revealed by disc-electrophoresis in polyacrylamide gel using 2-naphthyl phosphate (pH 4.0) as a substrate. No differences in the number of AcP electromorphs and their mobility were observed at both these temperatures. The total activity of AcP electromorphas per unit of cellular protein and their total thermostability were lower in amoebae acclimated to 10 degrees C than to 25 degrees C. The above decrease may be a consequence of a simultaneous decrease in the activity and thermostability of two tartrate-sensitive electromorphs, both being of lysosomal nature. The total activity and thermostability of tartrate-resistant AcP electromorphs did not differ in amoebae acclimated to the two above temperatures. In amoebae cultured at 10 degrees C the fall of activity and thermostability of lysosomal AcP correlates with the decrease in their primary cell thermoresistance and phagocytic activity. The obtained results confirm the earlier conclusion (Vysotskaya et al., 1994) that lysosomes may be involved in acclimation of electrothermal animals to changing environmental temperatures.
authors.affiliation: Institute of Cytology RAS, St. Petersburg. sopina@cit.ras.spb.ru
authors.forename: V A
authors.initials: VA
authors.lastname: Sopina
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism*; D000656:Amoeba / Q000201:enzymology*; D000818:Animals; D004589:Electrophoresis, Disc; D004795:Enzyme Stability; D013696:Temperature
chemical_list: D000135:Acid Phosphatase
vernacular_title: Chislo, aktivnost' i termostabil'nost' élektroforeticheskikh form kisloĭ fosfatazy u ameb Amoeba proteus, kul'tiviruemykh pri razlichnykh temperaturakh.