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Comparison of the (Ca2+ + Mg2+)-ATPase proteins from normal and dystrophic chicken sarcoplasmic reticulum
Abstract:
The involvement of membrane protein in dystrophic chicken fragmented sarcoplasmic reticulum alterations has been examined. A purified preparation of the (Ca2+ + Mg2+)-ATPase protein from dystrophic fragmented sarcoplasmic reticulum was found to have a reduced calcium-sensitive ATPase activity and phosphoenzyme level, in agreement with alterations found in dystrophic chicken fragmented sarcoplasmic reticulum. An amino acid analysis of the ATPase preparations showed no difference in the normal and dystrophic (Ca2+ + Mg2+)-ATPase. The (Ca2+ + Mg2+)-ATPase was investigated further by isoelectric focusing and proteolytic digestion of the fragmented sarcoplasmic reticulum. Neither of these methods indicated any alteration in the composition of the dystrophic (Ca2+ + Mg2+)-ATPase. We have concluded that the alterations observed in dystrophic fragmented sarcoplasmic reticulum are not due to increased amounts of non-(Ca2+ + Mg2+)-ATPase protein, and that the normal and dystrophic (Ca2+ + Mg2+)-ATPase protein are not detectably different.
Insights
Membrane protein alterations in dystrophic chicken sarcoplasmic reticulum were studied. The calcium-sensitive ATPase activity was reduced, but the (Ca2+ + Mg2+)-ATPase protein itself showed no detectable differences from normal.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Dystrophic chicken fragmented sarcoplasmic reticulum exhibits alterations.
- The role of membrane proteins in these alterations requires investigation.
Purpose of the Study:
- To examine the involvement of membrane protein, specifically (Ca2+ + Mg2+)-ATPase, in dystrophic chicken fragmented sarcoplasmic reticulum alterations.
- To determine if differences exist in the composition or activity of (Ca2+ + Mg2+)-ATPase between normal and dystrophic chickens.
Main Methods:
- Purification of (Ca2+ + Mg2+)-ATPase from normal and dystrophic fragmented sarcoplasmic reticulum.
- Assay of calcium-sensitive ATPase activity and phosphoenzyme levels.
- Amino acid analysis of purified ATPase preparations.
- Isoelectric focusing and proteolytic digestion of fragmented sarcoplasmic reticulum.
Main Results:
- Purified (Ca2+ + Mg2+)-ATPase from dystrophic fragmented sarcoplasmic reticulum showed reduced calcium-sensitive ATPase activity and phosphoenzyme levels.
- Amino acid analysis revealed no differences in the composition of normal and dystrophic (Ca2+ + Mg2+)-ATPase.
- Isoelectric focusing and proteolytic digestion did not indicate any compositional alterations in the dystrophic (Ca2+ + Mg2+)-ATPase.
Conclusions:
- The observed alterations in dystrophic fragmented sarcoplasmic reticulum are not attributable to increased amounts of non-(Ca2+ + Mg2+)-ATPase protein.
- The normal and dystrophic (Ca2+ + Mg2+)-ATPase proteins are not detectably different in composition.