Glycogen synthase, the enzyme that catalyzes the rate-limiting reaction of glycogen syntheses has been purified and characterized from Ascaris suum muscle. Glycogen in the crude extract was digested to release the enzyme, eluted from a DE52 cellulose column and then applied to a Sepharose affinity column. The purified Ascaris enzyme was found to be homologous to the mammalian enzyme with regard to subunit and holoenzyme Mr^3 allosteric activation, substrate affinity and covalent modification. However, the association between Ascaris glycogen synthase and endogenous glycogen differed from that in mammalian systems.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc798067 |
| Date | 08 1900 |
| Creators | Hannigan, Linda L. (Linda Lucile) |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights |
Page generated in 0.0024 seconds