The electrophoretic behavior of sarcoplasmic proteins was
investigated by the use of vertical acrylamide gel electrophoresis.
The first part of the study was concerned with the separation of
sarcoplasmic proteins extracted at different times of post-mortem
aging. Electrophoresis of the sarcoplasmic extracts by the discontinuous
technique, using ten percent acrylamide gels, resulted in
the separation of 18 (possibly 20) electrophoretically different proteins.
Differences between electrophoretic patterns of sarcoplasmic
proteins as post-mortem aging proceeded were slight.
Heterogeneity of sarcoplasmic protein fractions obtained by
DEAE-cellulose chromatography was investigated by vertical acrylamide
gel electrophoresis in the second part of this study. Electrophoretic
analyses of the sarcoplasmic fractions from the above
separations indicated that the major peaks of the chromatographic profiles were quite heterogeneous. Fraction Areas I and IV, which
appeared as single homogeneous chromatographic peaks, showed
five and six distinct bands, respectively, when subjected to gel
electrophoresis. Once again changes in the electrophoretic patterns
at 0 and 10 days of post-mortem aging were slight with main differences
being in the density of the bands.
The versatility and high resolving power of acrylamide gel
electrophoresis for separating sarcoplasmic proteins was demonstrated.
Excellent reproducibility of electrophoretic patterns was
noted and in most instances, the patterns were clear and showed
well-defined bands.
Attempts to fractionate sarcoplasmic proteins by density
gradient electrophoresis resulted in separations characterized by
poor resolution. / Graduation date: 1968
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/26802 |
| Date | 08 December 1967 |
| Creators | Petropakis, Heracles John |
| Contributors | Anglemier, Allen F. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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