Change in the structure of Shope papilloma virus-induced arginase associated with mutation of the virus.
The change in the state of the virus-induced enzyme associated with a mutation in the virus provides additional evidence that the enzyme is synthesized from virus rather than rabbit genetic information. This change in structure results in differences in stability of polymerization, degree of optical rotary dispersion (ORD) specific rotation, change in elution characteristics from carboxymethyl cellulose, and a reduction in specific activity of the arginase. Liver arginase differs markedly in ORD characteristics from the virus-induced enzyme. In contrast to the virus-induced enzyme, it showed no negative Cotton effect at 233 nm until it was activated with manganese. Manganese had no influence on the ORD spectrum of virus-induced arginase. In addition, liver arginase is denatured by 4 M urea, while the virus-induced enzyme requires 10 M urea for denaturation.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001119:Arginase / Q000032:analysis* / Q000302:isolation & purification; D004790:Enzyme Induction; D005827:Genetics, Microbial; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D008345:Manganese; D008970:Molecular Weight; D009154:Mutation; D009905:Optical Rotatory Dispersion; D027383:Papillomaviridae; D011489:Protein Denaturation; D011817:Rabbits; D014412:Tumor Virus Infections / Q000382:microbiology; D014508:Urea
D000596:Amino Acids; D008345:Manganese; D014508:Urea; D001119:Arginase