Advisor

W. Herman Taylor

Date of Award

8-6-1975

Document Type

Thesis

Degree Name

Master of Science (M.S.) in Biology

Department

Biology

Physical Description

1 online resource (49 p.)

Subjects

Zinc, Dihydroorotase

DOI

10.15760/etd.2015

Abstract

Dihydroorotase (4,4—dihydroorotic acid amidolyase, EC 3.5.2.3.) which catalyzes the reversible cyclization of N-carbamyl-L-aspartate to L-dihydroorotate has been purified from orotate-grown Clostridium oroticum. The enzyme is stable in 0.3 M sodium chloride and 10 µ ZnSO4. Sodium dodecyl sulfate gel electrophoresis indicates the enzyme to be composed of two identical subunits each with a molecular weight of 58,000 + 6000. Dihydroorotase is shown to be a zinc-containing metalloenzyme with 2 g atoms of zinc per 58,000 g of protein. The role of zinc in dihydroorotase is discussed.

Persistent Identifier

http://archives.pdx.edu/ds/psu/12787

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