Two direct methyltransferase systems in winter wheat have been reported using partially purified enzyme extracts. In order to gain further understanding of these enzymes, such classical enzyme investigations as pH range and optimum pH, the calculation of average activation energies, and inhibition investigations need to be undertaken using more highly purified enzymes. The purpose of this investigation was to develop procedures for further purification of S-methyl-Lmethionine:homocysteine methyltransferase in order that future researchers might undertake such studies.
| Identifer | oai:union.ndltd.org:BSU/oai:cardinalscholar.bsu.edu:handle/181385 |
| Date | January 1976 |
| Creators | Bryan, James E. |
| Contributors | Allamong, Betty D. |
| Source Sets | Ball State University |
| Detected Language | English |
| Format | vi, 45 leaves : ill. ; 28 cm. |
| Source | Virtual Press |
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