Gel electrophoretic analysis of bovine sarcoplasmic proteins Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/zs25xc01n

Descriptions

Attribute NameValues
Creator
Abstract or Summary
  • 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.
Resource Type
Date Available
Date Copyright
Date Issued
Degree Level
Degree Name
Degree Field
Degree Grantor
Commencement Year
Advisor
Academic Affiliation
Non-Academic Affiliation
Subject
Rights Statement
Peer Reviewed
Language
Digitization Specifications
  • File scanned at 300 ppi (Monochrome, 24-bit Color) using Scamax Scan+ V.1.0.32.10766 on a Scanmax 412CD by InoTec in PDF format. LuraDocument PDF Compressor V.5.8.71.50 used for pdf compression and textual OCR.
Replaces
Additional Information
  • description.provenance : Submitted by Erin Clark (ecscannerosu@gmail.com) on 2012-01-11T17:06:51Z No. of bitstreams: 1 PETROPAKISHERACLES1968.pdf: 1108481 bytes, checksum: 4f41cc5ee17701b5604d93e4619fa728 (MD5)
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-01-17T22:49:40Z (GMT) No. of bitstreams: 1 PETROPAKISHERACLES1968.pdf: 1108481 bytes, checksum: 4f41cc5ee17701b5604d93e4619fa728 (MD5)
  • description.provenance : Made available in DSpace on 2012-01-17T22:49:40Z (GMT). No. of bitstreams: 1 PETROPAKISHERACLES1968.pdf: 1108481 bytes, checksum: 4f41cc5ee17701b5604d93e4619fa728 (MD5) Previous issue date: 1967-12-08
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-01-11T21:17:32Z (GMT) No. of bitstreams: 1 PETROPAKISHERACLES1968.pdf: 1108481 bytes, checksum: 4f41cc5ee17701b5604d93e4619fa728 (MD5)

Relationships

In Administrative Set:
Last modified: 08/08/2017

Downloadable Content

Download PDF
Citations:

EndNote | Zotero | Mendeley

Items