title: Activity of aspartate transcarbamylase in uninfected and type 5 adenovirus-infected HeLa cells.
abstract: Consigli, Richard A. (University of Pennsylvania, Philadelphia), and Harold S. Ginsberg. Activity of aspartate transcarbamylase in uninfected and type 5 adenovirus-infected HeLa cells. J. Bacteriol. 87:1034-1043. 1964.-A two- to three-fold increase in aspartate transcarbamylase (ATCase) activity was observed in type 5 adenovirus-infected HeLa cells 18 hr after infection. The enhanced enzyme activity was virus-specific and dependent on biosynthesis of deoxyribonucleic acid and protein. When various characteristics as well as the kinetics of the enzymes from uninfected and infected cells were compared, ATCase from adenovirus-infected cells was shown to have an altered pH optimum, greater heat stability, increased maximal velocity, and increased K(m) value for aspartate.
mesh_terms: D000256:Adenoviridae / Q000201:enzymology*; D002845:Chromatography; D046508:Culture Techniques; D004247:DNA / Q000096:biosynthesis*; D005467:Floxuridine / Q000494:pharmacology*; D006367:HeLa Cells; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D014118:Toxins, Biological; D014166:Transferases / Q000378:metabolism*
chemical_list: D014118:Toxins, Biological; D005467:Floxuridine; D004247:DNA; D014166:Transferases