Purification of S-methyl-L-methionine : homocysteine methyltransferase in Triticum aestivum (Gramineae)

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dc.contributor.advisor Allamong, Betty D. en_US
dc.contributor.author Bryan, James E. en_US
dc.date.accessioned 2011-06-03T19:31:48Z
dc.date.available 2011-06-03T19:31:48Z
dc.date.created 1976 en_US
dc.date.issued 1976
dc.identifier LD2489.Z78 1976 .B79 en_US
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/handle/181385
dc.description.abstract 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.
dc.format.extent vi, 45 leaves : ill. ; 28 cm. en_US
dc.source Virtual Press en_US
dc.subject.lcsh Transmethylation. en_US
dc.subject.lcsh Methionine. en_US
dc.subject.lcsh Enzymes -- Synthesis. en_US
dc.subject.lcsh Wheat. en_US
dc.title Purification of S-methyl-L-methionine : homocysteine methyltransferase in Triticum aestivum (Gramineae) en_US
dc.description.degree Thesis (M.S.)
dc.identifier.cardcat-url http://liblink.bsu.edu/catkey/415888 en_US


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  • Master's Theses [5318]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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