Radiation inactivation of hepatic sulfite oxidase

Journal Article · Wed Jul 01 04:00:00 EDT 1987 · Arch. Biochem. Biophys.; (United States)

DOI:https://doi.org/10.1016/0003-9861(87)90444-9· OSTI ID:6071020

Barber, M J; Solomonson, L P; McCreery, M J

Sulfite oxidase purified from chicken liver, is comprised of two identical subunits of 55 kDa, each of which contains a molybdenum and heme prosthetic group. The functional size of sulfite oxidase was determined by radiation inactivation analysis using both full, sulfite:cytochrome c reductase, and partial, sulfite:ferricyanide reductase, catalytic activities. Inactivation of full enzyme activity indicated a target size of 42 kDa while the partial activity indicated a target size of 25 kDa. These results confirm the earlier findings of two equivalent subunits and suggest the presence of a functional domain within the subunit structure that contains the molybdenum center and exhibits a smaller molecular mass than that of the enzyme subunit.

• Research Organization: Univ. of South Florida, Tampa
• OSTI ID: 6071020
• Journal Information: Arch. Biochem. Biophys.; (United States), Journal Name: Arch. Biochem. Biophys.; (United States) Vol. 256:1; ISSN ABBIA
• Country of Publication: United States
• Language: English

Related Subjects

560120* -- Radiation Effects on Biochemicals
Cells
& Tissue Culture
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ANIMALS
BIOLOGICAL EFFECTS
BIOLOGICAL RADIATION EFFECTS
BIRDS
BODY
CHICKENS
DIGESTIVE SYSTEM
ELEMENTS
ENZYME ACTIVITY
ENZYMES
FOWL
GLANDS
LIVER
METALS
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
MOLYBDENUM
ORGANS
OXIDOREDUCTASES
RADIATION EFFECTS
TRANSITION ELEMENTS
VERTEBRATES