Hexokinase has been found in a soluble and a bound form in homogenates of Ascaris suum muscle. Cellulose acetate electrophoresis, isoelectric focusing, and ion exchange chromatography confirmed the presence of only one molecular form of hexokinase in this muscle. A procedure for purifying hexokinase from Ascaris muscle has been developed. The physical and catalytic properties of the enzyme are comparable to mammalian hexokinases. The enzyme is a monomer with a molecular weight of 100,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. The Michaelis constants for glucose and ATP are 4.7 x 10-3 M and 2.2 x 10-4 M, respectively. Ascaris' hexokinase also exhibits end-product inhibition by glucose 6-phosphate and ADP. It is postulated that the kinetic para meters of the enzyme are the results of its function, that of generating glucose 6-phosphate primarily for glycogen synthesis.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc798437 |
| Date | 08 1900 |
| Creators | Supowit, Scott C. |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | v, 61 leaves : ill., Text |
| Rights | Public, Supowit, Scott C., Copyright, Copyright is held by the author, unless otherwise noted. All rights |
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