Date of Award:

5-1973

Document Type:

Dissertation

Degree Name:

Doctor of Philosophy (PhD)

Department:

Plants, Soils, and Climate

Department name when degree awarded

Plant Nutrition and Biochemistry

Committee Chair(s)

Gene W. Miller

Committee

Gene W. Miller

Committee

Bruce F. Burnham

Committee

George W. Cochran

Committee

Raymond Lynn

Committee

D. K. Salunkhe

Committee

B. F. Burnham

Abstract

Uroporphyrinogen decarboxylase which catalyses the formation of coproporphyrinogen from uroporphyrinogen is located in the soluble fraction of tobacco leaves and was purified 72 fold through ammonium sulphate precipitation and calcium phosphate gel adsorption.

Kinetic studies indicated that the apparent Michaelis constant was 1 x 10-6 for uroporphyrinogen III (pH 6.5; 37° C). Uroporphyrinogen III served as a much better substrate than uroporphyrinogen I under the standard conditions of this study.

Enzyme activity was inhibited by thiol reagents and heavy divalent cations.

Both chloride and fluoride salts inhibited the formation of coproporphyrinogen from uroporphyrinogen.

Enzyme activity was inhibited by several metals and was stimulated by some chelating agents.

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