Kloss, Robert A.||Reynolds, Rosalie D.
M.S. (Master of Science)
Department of Chemistry
The enzyme, 2-hydroxy-6~methyl benzoic acid synthetase, was isolated and purified from the mold, Penicillium griseofulvum. by obtaining cell-free extracts and subjecting these to ammonium sulfate and acetone fractionation. Electrophoresis was done to observe the homogeneity of the final enzyme preparation. A chemical method for the synthesis of malonyl coenzyme-A was developed. The final enzyme preparation was tested for cofactor dependence by including studies with reduced triphosphopyridine nucleotide, adenosine triphosphate, biotin and manganese. A study comparing the reactivity of the purified enzyme with a substrate of malonic acid and sodium acetate to the reactivity of the purified enzyme with a substrate of malonyl coenzyme-A and acetyl coenzyme-A was included. Through these and other studies, it was concluded that this enzyme is responsible for the entire synthesis of 2-hydroxy-6-methyl benzoic acid, but does not contain the active sites necessary to convert acetyl coenzyme-A to malonyl coenzyme-A or to place the coenzyme-A onto the substrate acetate molecules.
Dickinson, Jack E., "Isolation and purification of 2-hydroxy-6-methyl benzoic acid synthetase from Penicillium griseofulvum" (1963). Graduate Research Theses & Dissertations. 3680.
vi, 44 pages
Northern Illinois University
Rights Statement 2
NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.